GCSH_THET8
ID GCSH_THET8 Reviewed; 128 AA.
AC Q5SKW9; P83697;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=TTHA0524;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), COFACTOR, MASS SPECTROMETRY,
RP SUBUNIT, AND LIPOYLATION AT LYS-63.
RX PubMed=12925792; DOI=10.1107/s0907444903014975;
RA Nakai T., Ishijima J., Masui R., Kuramitsu S., Kamiya N.;
RT "Structure of Thermus thermophilus HB8 H-protein of the glycine-cleavage
RT system, resolved by a six-dimensional molecular-replacement method.";
RL Acta Crystallogr. D 59:1610-1618(2003).
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:0000255|HAMAP-Rule:MF_00272}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00272,
CC ECO:0000269|PubMed:12925792};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|HAMAP-
CC Rule:MF_00272, ECO:0000269|PubMed:12925792};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H (By similarity). Monomer. {ECO:0000255|HAMAP-Rule:MF_00272,
CC ECO:0000269|PubMed:12925792}.
CC -!- MASS SPECTROMETRY: Mass=14083; Method=MALDI; Note=Unlipoylated
CC protein.; Evidence={ECO:0000269|PubMed:12925792};
CC -!- MASS SPECTROMETRY: Mass=14273; Method=MALDI; Note=Lipoylated protein.;
CC Evidence={ECO:0000269|PubMed:12925792};
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000255|HAMAP-
CC Rule:MF_00272}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008226; BAD70347.1; -; Genomic_DNA.
DR RefSeq; WP_011228002.1; NC_006461.1.
DR RefSeq; YP_143790.1; NC_006461.1.
DR PDB; 1ONL; X-ray; 2.50 A; A/B/C=1-128.
DR PDBsum; 1ONL; -.
DR AlphaFoldDB; Q5SKW9; -.
DR SMR; Q5SKW9; -.
DR STRING; 300852.55771906; -.
DR EnsemblBacteria; BAD70347; BAD70347; BAD70347.
DR GeneID; 3169107; -.
DR KEGG; ttj:TTHA0524; -.
DR PATRIC; fig|300852.9.peg.522; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_0_0; -.
DR OMA; YRDSHEW; -.
DR PhylomeDB; Q5SKW9; -.
DR EvolutionaryTrace; Q5SKW9; -.
DR Proteomes; UP000000532; 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 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 PANTHER; PTHR11715; PTHR11715; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR00527; gcvH; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipoyl; Reference proteome.
FT CHAIN 1..128
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000302458"
FT DOMAIN 22..104
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 63
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272,
FT ECO:0000269|PubMed:12925792"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1ONL"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1ONL"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1ONL"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1ONL"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1ONL"
FT STRAND 55..69
FT /evidence="ECO:0007829|PDB:1ONL"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:1ONL"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1ONL"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1ONL"
FT TURN 94..98
FT /evidence="ECO:0007829|PDB:1ONL"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1ONL"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:1ONL"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:1ONL"
SQ SEQUENCE 128 AA; 14083 MW; 9A93A6CA42B4DD4E CRC64;
MDIPKDRFYT KTHEWALPEG DTVLVGITDY AQDALGDVVY VELPEVGRVV EKGEAVAVVE
SVKTASDIYA PVAGEIVEVN LALEKTPELV NQDPYGEGWI FRLKPRDMGD LDELLDAGGY
QEVLESEA
