GCSH_THEMA
ID GCSH_THEMA Reviewed; 124 AA.
AC Q9WY55;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=TM_0212;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|HAMAP-
CC Rule:MF_00272};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00272}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000255|HAMAP-
CC Rule:MF_00272}.
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DR EMBL; AE000512; AAD35304.1; -; Genomic_DNA.
DR PIR; F72403; F72403.
DR RefSeq; NP_228027.1; NC_000853.1.
DR RefSeq; WP_010865076.1; NC_023151.1.
DR PDB; 1ZKO; X-ray; 1.65 A; A/B=1-124.
DR PDB; 2KA7; NMR; -; A=1-124.
DR PDBsum; 1ZKO; -.
DR PDBsum; 2KA7; -.
DR AlphaFoldDB; Q9WY55; -.
DR BMRB; Q9WY55; -.
DR SMR; Q9WY55; -.
DR STRING; 243274.THEMA_03665; -.
DR EnsemblBacteria; AAD35304; AAD35304; TM_0212.
DR KEGG; tma:TM0212; -.
DR eggNOG; COG0509; Bacteria.
DR InParanoid; Q9WY55; -.
DR OMA; YRDSHEW; -.
DR EvolutionaryTrace; Q9WY55; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
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..124
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000166258"
FT DOMAIN 19..101
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 60
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1ZKO"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:1ZKO"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1ZKO"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1ZKO"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1ZKO"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1ZKO"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1ZKO"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1ZKO"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1ZKO"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:1ZKO"
FT TURN 91..95
FT /evidence="ECO:0007829|PDB:1ZKO"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1ZKO"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:1ZKO"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:1ZKO"
SQ SEQUENCE 124 AA; 13915 MW; 90B7CDE430A16C9F CRC64;
MKMKKYTKTH EWVSIEDKVA TVGITNHAQE QLGDVVYVDL PEVGREVKKG EVVASIESVK
AAADVYAPLS GKIVEVNEKL DTEPELINKD PEGEGWLFKM EISDEGELED LLDEQAYQEF
CAQE
