ID   A0A0N5BVS5_STREA        Unreviewed;       159 AA.
AC   A0A0N5BVS5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000993100.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000993100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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; A0A0N5BVS5; -.
DR   STRING; 174720.A0A0N5BVS5; -.
DR   WBParaSite; SPAL_0000993100.1; SPAL_0000993100.1; SPAL_0000993100.
DR   Proteomes; UP000046392; Unplaced.
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   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU364055}.
FT   DOMAIN          51..133
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         92
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   159 AA;  17879 MW;  E2EBFC71333BA5C7 CRC64;
     MFGTRVFALL PFSSKIVKVN SINHILQTVR NCSTGRFYTK KHEWVVINKE IGTVGISDYA
     QESLGDIVYV ELPEVGTNVE RGDAVGTIES VKAASDVYTP ISGKVHEVNE TATDEPNIIN
     KSPYEKGWLF KIILSNPEEL KELMNEEAYE KFKQEEGDH
//