GCSH_CLOD6
ID GCSH_CLOD6 Reviewed; 125 AA.
AC Q189S4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=CD630_07290;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ67563.1; -; Genomic_DNA.
DR RefSeq; WP_003418363.1; NZ_CP010905.2.
DR RefSeq; YP_001087206.1; NC_009089.1.
DR AlphaFoldDB; Q189S4; -.
DR SMR; Q189S4; -.
DR STRING; 272563.CD630_07290; -.
DR PRIDE; Q189S4; -.
DR EnsemblBacteria; CAJ67563; CAJ67563; CD630_07290.
DR GeneID; 66353234; -.
DR KEGG; cdf:CD630_07290; -.
DR KEGG; pdc:CDIF630_00845; -.
DR PATRIC; fig|272563.120.peg.750; -.
DR eggNOG; COG0509; Bacteria.
DR OMA; EHEWLSG; -.
DR PhylomeDB; Q189S4; -.
DR BioCyc; PDIF272563:G12WB-840-MON; -.
DR Proteomes; UP000001978; 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; 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.
PE 3: Inferred from homology;
KW Lipoyl; Reference proteome.
FT CHAIN 1..125
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000302367"
FT DOMAIN 23..104
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 64
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ SEQUENCE 125 AA; 14047 MW; AC4594D92CCE8A69 CRC64;
MKLLPELKYS KDHEWVKVID GDVVYIGITD YAQDQLGEIL FVETPEVEDT VTKGVDFGVV
ESSKVASDLI SPVNGEVLEV NEKLEDEPEC INEDPYENWI LKVKLADVAE LDTLLSDKEY
EAGLE
