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Database: UniProt
Entry: W0HUI5_9GAMM
LinkDB: W0HUI5_9GAMM
Original site: W0HUI5_9GAMM 
ID   W0HUI5_9GAMM            Unreviewed;       131 AA.
AC   W0HUI5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gvcH {ECO:0000313|EMBL:AHF75870.1};
GN   Synonyms=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN   ORFNames=Sant_0780 {ECO:0000313|EMBL:AHF75870.1};
OS   Sodalis praecaptivus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF75870.1, ECO:0000313|Proteomes:UP000019028};
RN   [1] {ECO:0000313|EMBL:AHF75870.1, ECO:0000313|Proteomes:UP000019028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 {ECO:0000313|EMBL:AHF75870.1,
RC   ECO:0000313|Proteomes:UP000019028};
RX   PubMed=24407854; DOI=10.1093/gbe/evt210;
RA   Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA   Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA   Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT   "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL   Genome Biol. Evol. 6:76-93(2014).
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; CP006569; AHF75870.1; -; Genomic_DNA.
DR   RefSeq; WP_025420999.1; NZ_CP006569.1.
DR   AlphaFoldDB; W0HUI5; -.
DR   KEGG; sod:Sant_0780; -.
DR   PATRIC; fig|1239307.3.peg.837; -.
DR   HOGENOM; CLU_097408_2_1_6; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000019028; 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:SF41; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019028}.
FT   DOMAIN          24..106
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         65
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT                   ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   131 AA;  13977 MW;  47304D316B5CE31A CRC64;
     MSNVPTELKY TASHEWVLNE GDGVYCVGIT EHAQELLGDM VFMDLPEVGA SFSAGEDCAV
     AESVKAASDI YAPISGEIVA VNDDLDGSPE LVNSAPYTDG WLFKIKAADE SEVNELLDAA
     AYQAAIDEED E
//
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