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Database: UniProt
Entry: G8NV46_GRAMM
LinkDB: G8NV46_GRAMM
Original site: G8NV46_GRAMM 
ID   G8NV46_GRAMM            Unreviewed;       128 AA.
AC   G8NV46;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN   OrderedLocusNames=AciX8_0988 {ECO:0000313|EMBL:AEU35335.1};
OS   Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU35335.1, ECO:0000313|Proteomes:UP000007113};
RN   [1] {ECO:0000313|EMBL:AEU35335.1, ECO:0000313|Proteomes:UP000007113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC   {ECO:0000313|Proteomes:UP000007113};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA   Haggblom M., Woyke T.;
RT   "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL   Submitted (NOV-2011) 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; CP003130; AEU35335.1; -; Genomic_DNA.
DR   RefSeq; WP_014264217.1; NC_016631.1.
DR   AlphaFoldDB; G8NV46; -.
DR   STRING; 682795.AciX8_0988; -.
DR   KEGG; gma:AciX8_0988; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_2_0; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000007113; Chromosome.
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:SF41; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007113}.
FT   DOMAIN          22..103
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         63
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT                   ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   128 AA;  13851 MW;  419AB3FEC83CCCC9 CRC64;
     MSYPENYRYA KSHEWLEIDG KTGIIGITDY AQSSLGDIVF VELPKVGDKL DAGSSFGSVE
     SVKAVSELYS PAAGTVIEIN EALNDEPETI NTDANETWII KLSLTGGESD DLLSAADYEK
     FVAEETGH
//
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