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Database: UniProt
Entry: A0A0K6HAL1_9GAMM
LinkDB: A0A0K6HAL1_9GAMM
Original site: A0A0K6HAL1_9GAMM 
ID   A0A0K6HAL1_9GAMM        Unreviewed;       129 AA.
AC   A0A0K6HAL1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN   ORFNames=Ga0061064_1950 {ECO:0000313|EMBL:CUA87795.1};
OS   Pseudidiomarina woesei.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Pseudidiomarina.
OX   NCBI_TaxID=1381080 {ECO:0000313|EMBL:CUA87795.1, ECO:0000313|Proteomes:UP000182598};
RN   [1] {ECO:0000313|Proteomes:UP000182598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27808 {ECO:0000313|Proteomes:UP000182598};
RA   Varghese N.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00272};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000256|HAMAP-
CC       Rule:MF_00272};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC       ECO:0000256|HAMAP-Rule:MF_00272}.
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DR   EMBL; CYHB01000006; CUA87795.1; -; Genomic_DNA.
DR   RefSeq; WP_055439592.1; NZ_LIPW01000006.1.
DR   AlphaFoldDB; A0A0K6HAL1; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000182598; Unassembled WGS sequence.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
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; 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.
PE   3: Inferred from homology;
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|HAMAP-Rule:MF_00272}.
FT   DOMAIN          24..106
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         65
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT                   ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   129 AA;  13911 MW;  AA5BA6A8AA2E59D4 CRC64;
     MSNIPKELKY ASTHEWVRNE GDGIFTVGIT EHAQDLLGDM VFVELPEVGD AVAAGDDVAV
     CESVKAASDI YAPIAGEIVE VNEELEDAPE TVNNDPFGDG WLFKIKAEDP SEVEGLLDAE
     GYQAVIDED
//
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