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GCSH2_SACS2
ID   GCSH2_SACS2             Reviewed;         148 AA.
AC   Q97Z69;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=SSO1061;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; AE006641; AAK41324.1; -; Genomic_DNA.
DR   PIR; E90258; E90258.
DR   RefSeq; WP_009989890.1; NC_002754.1.
DR   AlphaFoldDB; Q97Z69; -.
DR   SMR; Q97Z69; -.
DR   STRING; 273057.SSO1061; -.
DR   EnsemblBacteria; AAK41324; AAK41324; SSO1061.
DR   GeneID; 44129994; -.
DR   KEGG; sso:SSO1061; -.
DR   PATRIC; fig|273057.12.peg.1057; -.
DR   eggNOG; arCOG01303; Archaea.
DR   HOGENOM; CLU_097408_2_2_2; -.
DR   InParanoid; Q97Z69; -.
DR   OMA; NTVWAKQ; -.
DR   PhylomeDB; Q97Z69; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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="Probable glycine cleavage system H protein 2"
FT                   /id="PRO_0000166283"
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   148 AA;  16299 MW;  813A7EA090AF0542 CRC64;
     MVVESNCEIP ENLYYFIEGK NTVWAKLESP DTIVVGITDL AQTMAGKIVK VRIKKKGTKV
     EKGRPVATME SGKWAGPVPA PVTGEVVEVN AEAEKSPIII NQDPYGKGWL VKMKMSNPEE
     LKQLFSGQAA IQKLKELIAS EKLTCKRL
 
 
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