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Database: UniProt
Entry: A0A0E0JW37_ORYPU
LinkDB: A0A0E0JW37_ORYPU
Original site: A0A0E0JW37_ORYPU 
ID   A0A0E0JW37_ORYPU        Unreviewed;       230 AA.
AC   A0A0E0JW37;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G04540.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC02G04540.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC02G04540.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0JW37; -.
DR   STRING; 4537.A0A0E0JW37; -.
DR   EnsemblPlants; OPUNC02G04540.1; OPUNC02G04540.1; OPUNC02G04540.
DR   Gramene; OPUNC02G04540.1; OPUNC02G04540.1; OPUNC02G04540.
DR   eggNOG; KOG3373; Eukaryota.
DR   HOGENOM; CLU_097408_0_0_1; -.
DR   OMA; MSHITFH; -.
DR   Proteomes; UP000026962; Chromosome 2.
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|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU364055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU364055}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..230
FT                   /note="Glycine cleavage system H protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002364536"
FT   DOMAIN          121..203
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          30..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         162
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   230 AA;  25717 MW;  B0AEE105BB7A7055 CRC64;
     MFFFLQFATC TTNLFCILLN IFTKEILEEE PPNPRTHREK ERDQRRERER SAARRRGAIQ
     FQSIPPRPRR PIVAMAASRL LWASRAASYL KISTFPRAFS TVLKDLKYAD THEWVKVEGD
     SATVGITDHA QHHLGDVVYV ELPEVGSSVS QGKNFGAVES VKATSDINSP VSGEVVAVND
     GLGDEPGLVN TSPYESGWII KVKVSDSGEL NSLMDDAKYS KFCEEEDSKH
//
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