ID   GCSH3_DICDI             Reviewed;         149 AA.
AC   Q54JU3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Putative glycine cleavage system H protein 3;
GN   Name=gcvH3; Synonyms=gcvH; ORFNames=DDB_G0287791;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(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 (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
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DR   EMBL; AAFI02000104; EAL63542.1; -; Genomic_DNA.
DR   RefSeq; XP_637059.1; XM_631967.1.
DR   AlphaFoldDB; Q54JU3; -.
DR   SMR; Q54JU3; -.
DR   STRING; 44689.DDB0231214; -.
DR   PaxDb; Q54JU3; -.
DR   PRIDE; Q54JU3; -.
DR   EnsemblProtists; EAL63542; EAL63542; DDB_G0287791.
DR   GeneID; 8626313; -.
DR   KEGG; ddi:DDB_G0287791; -.
DR   dictyBase; DDB_G0287791; gcvH3.
DR   eggNOG; KOG3373; Eukaryota.
DR   HOGENOM; CLU_097408_2_0_1; -.
DR   InParanoid; Q54JU3; -.
DR   OMA; ESHEWIK; -.
DR   PhylomeDB; Q54JU3; -.
DR   PRO; PR:Q54JU3; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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   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.
PE   3: Inferred from homology;
KW   Lipoyl; Reference proteome.
FT   CHAIN           1..149
FT                   /note="Putative glycine cleavage system H protein 3"
FT                   /id="PRO_0000328549"
FT   DOMAIN          39..121
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         80
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   149 AA;  17004 MW;  345BD7B0162ABB98 CRC64;
     MISNFLKSNN IKNNSPFRSF CTRYSESHEW IKFNHRNKTC TLGITKYASD QLKSIVNINL
     PDLNSTITRK QPFGNIESTK TVADLFSDVD GKAVLLNSDV IVDPTIVSHS PEDKGWLIKM
     ESNDFESFNK MMTKSEYGQF LKDINKSNV