ID   GCSH3_AQUAE             Reviewed;         161 AA.
AC   O67080;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Glycine cleavage system H protein 3 {ECO:0000255|HAMAP-Rule:MF_00272};
GN   Name=gcvH3 {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=aq_944;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07053.1; -; Genomic_DNA.
DR   PIR; E70381; E70381.
DR   RefSeq; NP_213643.1; NC_000918.1.
DR   RefSeq; WP_010880581.1; NC_000918.1.
DR   AlphaFoldDB; O67080; -.
DR   SMR; O67080; -.
DR   STRING; 224324.aq_944; -.
DR   EnsemblBacteria; AAC07053; AAC07053; aq_944.
DR   KEGG; aae:aq_944; -.
DR   PATRIC; fig|224324.8.peg.740; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_2_0; -.
DR   InParanoid; O67080; -.
DR   OMA; GKWAGPI; -.
DR   OrthoDB; 1773485at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR   GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
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; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR11715; PTHR11715; 1.
DR   Pfam; PF01597; GCV_H; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Lipoyl; Reference proteome.
FT   CHAIN           1..161
FT                   /note="Glycine cleavage system H protein 3"
FT                   /id="PRO_0000166199"
FT   DOMAIN          40..122
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         81
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ   SEQUENCE   161 AA;  18106 MW;  92C6DD5AB4E45B8D CRC64;
     MGKQEKDLGT AWEYQGCLIP KDLYYDIENQ VWVRVNEDGT VTLGLTDVGQ TRAGRLLHIR
     VKPVGTKVKK GKPVATLESG KWAGPVPALV EGEIVEVNPK VVEDPNYINI DPYGDAWIVK
     IKPTSEETLK RDLSELAHGE KAHEEMKKHI DEWDIVCMRC V