ID   GCSH5_AQUAE             Reviewed;         148 AA.
AC   O66720;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Glycine cleavage system H protein 5 {ECO:0000255|HAMAP-Rule:MF_00272};
GN   Name=gcvH5 {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=aq_402;
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; AAC06682.1; -; Genomic_DNA.
DR   PIR; D70336; D70336.
DR   RefSeq; NP_213280.1; NC_000918.1.
DR   RefSeq; WP_010880218.1; NC_000918.1.
DR   AlphaFoldDB; O66720; -.
DR   SMR; O66720; -.
DR   STRING; 224324.aq_402; -.
DR   EnsemblBacteria; AAC06682; AAC06682; aq_402.
DR   KEGG; aae:aq_402; -.
DR   PATRIC; fig|224324.8.peg.330; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_2_0; -.
DR   InParanoid; O66720; -.
DR   OMA; EANAFTW; -.
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..148
FT                   /note="Glycine cleavage system H protein 5"
FT                   /id="PRO_0000166201"
FT   DOMAIN          33..115
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         74
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ   SEQUENCE   148 AA;  15823 MW;  F132705712920BCD CRC64;
     MAEVNGCQLP EDRLYYINPD KNAFIWAKEE DGVFTIGLTS VAAAMAGRLV AYTPKKVGKA
     VKKDKSVATI ESGKWVGPVP SPFDGEIVEV NEALKGNPAL VNDDPYGQGW IAKVKPANPE
     EAKSVLVDAN KAAELLQPIV QEKGVKCG