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Entry: A0A0U3HU94_9MICC
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ID   A0A0U3HU94_9MICC        Unreviewed;       126 AA.
AC   A0A0U3HU94;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH_1 {ECO:0000313|EMBL:GEO92864.1};
GN   Synonyms=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN   ORFNames=AS188_00360 {ECO:0000313|EMBL:ALU38455.1}, AUQ48_06940
GN   {ECO:0000313|EMBL:PLC12014.1}, KFL01_21700
GN   {ECO:0000313|EMBL:GEO92864.1};
OS   Kocuria flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU38455.1, ECO:0000313|Proteomes:UP000057181};
RN   [1] {ECO:0000313|EMBL:ALU38455.1, ECO:0000313|Proteomes:UP000057181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO-9041 {ECO:0000313|EMBL:ALU38455.1,
RC   ECO:0000313|Proteomes:UP000057181};
RA   Zhou M., Dai J.;
RT   "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PLC12014.1, ECO:0000313|Proteomes:UP000234632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S43 {ECO:0000313|EMBL:PLC12014.1,
RC   ECO:0000313|Proteomes:UP000234632};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:GEO92864.1, ECO:0000313|Proteomes:UP000321155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO92864.1,
RC   ECO:0000313|Proteomes:UP000321155};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL   Submitted (JUL-2019) 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; CP013254; ALU38455.1; -; Genomic_DNA.
DR   EMBL; BJZR01000066; GEO92864.1; -; Genomic_DNA.
DR   EMBL; LOMZ01000001; PLC12014.1; -; Genomic_DNA.
DR   RefSeq; WP_058857169.1; NZ_LOMZ01000001.1.
DR   AlphaFoldDB; A0A0U3HU94; -.
DR   STRING; 446860.AS188_00360; -.
DR   KEGG; kfv:AS188_00360; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000057181; Chromosome.
DR   Proteomes; UP000234632; Unassembled WGS sequence.
DR   Proteomes; UP000321155; 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: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:UP000057181}.
FT   DOMAIN          22..104
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   126 AA;  13101 MW;  D4B8938A41DF1C14 CRC64;
     MSTVLPDLRY SAEHEWIDSA SPARIGISQV AVDALGDVVY LDLPEAGSTV TAGEVCGEVE
     STKSVSELFS PVTGTVVEVN AEAVDNPAVL NEDPYGAGWL FTVEVSEEGP LLSAQEYADA
     NGGELG
//
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