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Database: UniProt
Entry: A0A1X4NGJ5_9PROT
LinkDB: A0A1X4NGJ5_9PROT
Original site: A0A1X4NGJ5_9PROT 
ID   A0A1X4NGJ5_9PROT        Unreviewed;       125 AA.
AC   A0A1X4NGJ5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=THS27_00525 {ECO:0000313|EMBL:OSQ46354.1};
OS   Thalassospira sp. MCCC 1A01428.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1470575 {ECO:0000313|EMBL:OSQ46354.1, ECO:0000313|Proteomes:UP000193740};
RN   [1] {ECO:0000313|EMBL:OSQ46354.1, ECO:0000313|Proteomes:UP000193740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A01428 {ECO:0000313|EMBL:OSQ46354.1,
RC   ECO:0000313|Proteomes:UP000193740};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thalassospira sp. MCCC 1A01428.";
RL   Submitted (MAR-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OSQ46354.1}.
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DR   EMBL; JFJZ01000001; OSQ46354.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X4NGJ5; -.
DR   STRING; 1470575.THS27_00525; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000193740; 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; 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|HAMAP-Rule:MF_00272}.
FT   DOMAIN          18..100
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         59
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT                   ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   125 AA;  13555 MW;  48B8C7E14A721BF9 CRC64;
     MAKKFSKEHE WLEIDGDVAT VGITDHAQQA LGDIVYVELP EVGKKLAKDG DAAVVESVKA
     ASDVYAPVDG EIVEANEELD ANPALVNESP ENDGWFFKIK ITDASQLDDL MDEAGYKAFV
     EGLED
//
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