ID   GCSH_OCEIH              Reviewed;         126 AA.
AC   Q8ENT9;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
DE   AltName: Full=Octanoyl/lipoyl carrier protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=OB2388;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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   -!- FUNCTION: Is also involved in protein lipoylation via its role as an
CC       octanoyl/lipoyl carrier protein intermediate. {ECO:0000255|HAMAP-
CC       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; BA000028; BAC14344.1; -; Genomic_DNA.
DR   RefSeq; WP_011066779.1; NC_004193.1.
DR   AlphaFoldDB; Q8ENT9; -.
DR   SMR; Q8ENT9; -.
DR   STRING; 221109.22778074; -.
DR   EnsemblBacteria; BAC14344; BAC14344; BAC14344.
DR   KEGG; oih:OB2388; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_2_9; -.
DR   OMA; EHEWLSG; -.
DR   OrthoDB; 1773485at2; -.
DR   PhylomeDB; Q8ENT9; -.
DR   Proteomes; UP000000822; 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   GO; GO:0009249; P:protein lipoylation; 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_0000166232"
FT   DOMAIN          22..104
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         63
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ   SEQUENCE   126 AA;  14356 MW;  FC25D78CBA917AA8 CRC64;
     MSLPQDLLYS KEHEWVKQED GKLRIGITDF AQDELGDIVF VELPEIGEEL KVDDPFGSVE
     SVKTVSELYA PVSGKVVEIN DDLEDSPEYV NESPYEKAWM IVIEPSDEKE LEELLSAENY
     EAFIQD