ID   GCSH_XYLFM              Reviewed;         131 AA.
AC   B0U269;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272};
GN   OrderedLocusNames=Xfasm12_0154;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA11191.1; -; Genomic_DNA.
DR   RefSeq; WP_004085045.1; NC_010513.1.
DR   AlphaFoldDB; B0U269; -.
DR   SMR; B0U269; -.
DR   KEGG; xfm:Xfasm12_0154; -.
DR   HOGENOM; CLU_097408_2_2_6; -.
DR   OMA; YRDSHEW; -.
DR   OrthoDB; 1773485at2; -.
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   3: Inferred from homology;
KW   Lipoyl.
FT   CHAIN           1..131
FT                   /note="Glycine cleavage system H protein"
FT                   /id="PRO_1000114564"
FT   DOMAIN          24..106
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         65
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ   SEQUENCE   131 AA;  14392 MW;  882563D40EB2D9EA CRC64;
     MSDIPGDLKF LKSHEWVRIE DNNRAIVGIS DHAQNLLGDL VYVELPNIGD HLDAGATAAV
     IESVKAASDI YSPVTGKVIE VNTTLSDKPE TINEDPYGEG WIMVIEMQAP EEISDLLSPD
     DYTEVLESDE H