ID   GCSH2_SULAC             Reviewed;         149 AA.
AC   Q4JBR3;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Probable glycine cleavage system H protein 2 {ECO:0000255|HAMAP-Rule:MF_00272};
GN   Name=gcvH2 {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=Saci_0350;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(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; CP000077; AAY79766.1; -; Genomic_DNA.
DR   RefSeq; WP_011277268.1; NC_007181.1.
DR   AlphaFoldDB; Q4JBR3; -.
DR   SMR; Q4JBR3; -.
DR   STRING; 330779.Saci_0350; -.
DR   EnsemblBacteria; AAY79766; AAY79766; Saci_0350.
DR   GeneID; 3473128; -.
DR   KEGG; sai:Saci_0350; -.
DR   PATRIC; fig|330779.12.peg.346; -.
DR   eggNOG; arCOG01303; Archaea.
DR   HOGENOM; CLU_097408_2_2_2; -.
DR   OMA; NTVWAKQ; -.
DR   Proteomes; UP000001018; 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; 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..149
FT                   /note="Probable glycine cleavage system H protein 2"
FT                   /id="PRO_0000166280"
FT   DOMAIN          32..114
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         73
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ   SEQUENCE   149 AA;  16445 MW;  6776F4E4D809BC45 CRC64;
     MVVEANCEIP ENLYYYIDGK NTVWVKIEGS DIAVVGITDL AQTMAGKIVK IRIKKKGIKV
     ERGRPVATLE SGKWAGPVPA PVSGEVVDSN SEVEKSPVIL NRDPYGQGWI AKIKISNQEE
     VKQLLTGQQA IQKLKEIITS EKLTCKRLQ