ID   A0A1W2PS29_HUMAN        Unreviewed;       197 AA.
AC   A0A1W2PS29;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000492798, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000492798, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [2] {ECO:0000313|Ensembl:ENSP00000492798}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (APR-2017) to UniProtKB.
CC   -!- FUNCTION: The H protein shuttles the methylamine group of glycine
CC       from the P protein to the T protein.
CC       {ECO:0000256|RuleBase:RU364055}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU364055};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000256|RuleBase:RU364055};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H. {ECO:0000256|RuleBase:RU364055}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion
CC       {ECO:0000256|RuleBase:RU364055}.
CC   -!- SIMILARITY: Belongs to the GcvH family.
CC       {ECO:0000256|RuleBase:RU364055}.
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DR   EMBL; AC092718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; A0A1W2PS29; -.
DR   BioMuta; ENSG00000284512; -.
DR   jPOST; A0A1W2PS29; -.
DR   PeptideAtlas; A0A1W2PS29; -.
DR   Ensembl; ENST00000640345; ENSP00000492798; ENSG00000284512.
DR   GeneCards; ENSG00000284512; -.
DR   GeneTree; ENSGT00390000011666; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IPR017453; GCV_H_sub.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR11715; PTHR11715; 1.
DR   Pfam; PF01597; GCV_H; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR00527; gcvH; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Lipoyl {ECO:0000256|PIRSR:PIRSR617453-50,
KW   ECO:0000256|RuleBase:RU364055};
KW   Mitochondrion {ECO:0000256|RuleBase:RU364055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transit peptide {ECO:0000256|RuleBase:RU364055}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    197       Glycine cleavage system H protein.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012054479.
FT   DOMAIN       66    146       Lipoyl-binding.
FT                                {ECO:0000259|PROSITE:PS50968}.
FT   MOD_RES     107    107       N6-lipoyllysine.
FT                                {ECO:0000256|PIRSR:PIRSR617453-50}.
SQ   SEQUENCE   197 AA;  21151 MW;  F890DE2157690E35 CRC64;
     MALRVVRSVR ALLCTLRAVP SPAAPCPPRP WQLGVGAVRT LRTGPALLSV RKFTEKHEWV
     TTENGIGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQDEF GALESVKAAS ELYSPLSGEV
     TEINEALAEN PGLVNKSCYE DALEVKRNET AGLRSRCQQG CIPSQGSRGE SVHLPFPASR
     GCLHSLACGP FLHLQNQ
//