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Database: UniProt
Entry: A0A1A6C6J0_9GAMM
LinkDB: A0A1A6C6J0_9GAMM
Original site: A0A1A6C6J0_9GAMM 
ID   A0A1A6C6J0_9GAMM        Unreviewed;       145 AA.
AC   A0A1A6C6J0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=Thpro_021226 {ECO:0000313|EMBL:OBS10176.1};
OS   Acidihalobacter prosperus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=160660 {ECO:0000313|EMBL:OBS10176.1, ECO:0000313|Proteomes:UP000029273};
RN   [1] {ECO:0000313|EMBL:OBS10176.1, ECO:0000313|Proteomes:UP000029273}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5130 {ECO:0000313|EMBL:OBS10176.1,
RC   ECO:0000313|Proteomes:UP000029273};
RX   PubMed=25342676;
RA   Ossandon F.J., Cardenas J.P., Corbett M., Quatrini R., Holmes D.S.,
RA   Watkin E.;
RT   "Draft Genome Sequence of the Iron-Oxidizing, Acidophilic, and Halotolerant
RT   'Thiobacillus prosperus' Type Strain DSM 5130.";
RL   Genome Announc. 2:0-0(2014).
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|HAMAP-
CC       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:OBS10176.1}.
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DR   EMBL; JQSG02000002; OBS10176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A6C6J0; -.
DR   STRING; 160660.BJI67_04100; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000029273; 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; IPR011053; Single_hybrid_motif.
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|HAMAP-Rule:MF_00272};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029273}.
FT   DOMAIN          30..112
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         71
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272"
SQ   SEQUENCE   145 AA;  15031 MW;  322C97637686DCA4 CRC64;
     MGAVRGCNIP EDLMYSVDNN VWVRQESDGS ATVGLTSYAC SLAGQIVSYT PKKVGKDVKK
     DKSCATVESG KWVGPAKAPV AGEVIAINDA VSAQPGLINE DPYGEGWLVK IKPADWSGDS
     ADLTTGADAL AAFEAKMEAD GFGGC
//
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