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Database: UniProt
Entry: A0A091ULY3_NIPNI
LinkDB: A0A091ULY3_NIPNI
Original site: A0A091ULY3_NIPNI 
ID   A0A091ULY3_NIPNI        Unreviewed;       120 AA.
AC   A0A091ULY3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
DE   Flags: Fragment;
GN   ORFNames=Y956_11431 {ECO:0000313|EMBL:KFQ91342.1};
OS   Nipponia nippon (Crested ibis) (Ibis nippon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC   Nipponia.
OX   NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ91342.1, ECO:0000313|Proteomes:UP000053283};
RN   [1] {ECO:0000313|EMBL:KFQ91342.1, ECO:0000313|Proteomes:UP000053283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ91342.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The H protein shuttles the methylamine group of glycine from
CC       the P protein to the T protein. {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: P,
CC       T, L and H. {ECO:0000256|RuleBase:RU364055}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU364055}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC       ECO:0000256|RuleBase:RU364055}.
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DR   EMBL; KL409709; KFQ91342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091ULY3; -.
DR   STRING; 128390.A0A091ULY3; -.
DR   eggNOG; KOG3373; Eukaryota.
DR   Proteomes; UP000053283; Unassembled WGS sequence.
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   Gene3D; 2.40.50.100; -; 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   NCBIfam; TIGR00527; gcvH; 1.
DR   PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR   PANTHER; PTHR11715:SF3; GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01597; GCV_H; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|PIRSR:PIRSR617453-50};
KW   Mitochondrion {ECO:0000256|RuleBase:RU364055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053283};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU364055}.
FT   DOMAIN          17..99
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         58
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ91342.1"
FT   NON_TER         120
FT                   /evidence="ECO:0000313|EMBL:KFQ91342.1"
SQ   SEQUENCE   120 AA;  13240 MW;  2F86B99401C1624C CRC64;
     ARKFTDKHEW ISVENGIGTV GISNFAQEAL GDIVYCSLPE VGTKLNKHDE FGALESVKAA
     SELYCPFSGE VTEINAALAD NPGLVNKSCY QDGWLIKMTA ELDDLMNEDA YEKYIKSIED
//
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