ID   GCSH_PELUB              Reviewed;         126 AA.
AC   Q4FMV2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=SAR11_0667;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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; CP000084; AAZ21487.1; -; Genomic_DNA.
DR   RefSeq; WP_006997244.1; NC_007205.1.
DR   AlphaFoldDB; Q4FMV2; -.
DR   SMR; Q4FMV2; -.
DR   STRING; 335992.SAR11_0667; -.
DR   EnsemblBacteria; AAZ21487; AAZ21487; SAR11_0667.
DR   GeneID; 66295171; -.
DR   KEGG; pub:SAR11_0667; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_2_5; -.
DR   OMA; YRDSHEW; -.
DR   OrthoDB; 1773485at2; -.
DR   Proteomes; UP000002528; 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   3: Inferred from homology;
KW   Lipoyl; Reference proteome.
FT   CHAIN           1..126
FT                   /note="Glycine cleavage system H protein"
FT                   /id="PRO_0000302405"
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"
SQ   SEQUENCE   126 AA;  13889 MW;  8FC881FE29D44473 CRC64;
     MSEVKYSKEH EWIKLDGDTA VVGITQHATE MLGDIVFVEL PEIGSSVVKD GNAGVVESTK
     AASDIYTPVS GEIIENNQAI VDDPAKVNSD PENEAWFFKL KITDKSEMDS LMNKEEYEKF
     SKESGS