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Database: UniProt
Entry: A0A1Q4H8U0_9MYCO
LinkDB: A0A1Q4H8U0_9MYCO
Original site: A0A1Q4H8U0_9MYCO 
ID   A0A1Q4H8U0_9MYCO        Unreviewed;       131 AA.
AC   A0A1Q4H8U0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272,
GN   ECO:0000313|EMBL:PEG55657.1};
GN   ORFNames=BRW64_19690 {ECO:0000313|EMBL:OJZ63958.1}, BV510_02170
GN   {ECO:0000313|EMBL:OPE55999.1}, CRI78_05200
GN   {ECO:0000313|EMBL:PEG55657.1};
OS   Mycolicibacterium diernhoferi.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1801 {ECO:0000313|EMBL:OJZ63958.1, ECO:0000313|Proteomes:UP000186837};
RN   [1] {ECO:0000313|EMBL:OPE55999.1, ECO:0000313|Proteomes:UP000191039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM1 {ECO:0000313|EMBL:OPE55999.1,
RC   ECO:0000313|Proteomes:UP000191039};
RA   Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RT   "genome sequences of unsequenced Mycobacteria.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OJZ63958.1, ECO:0000313|Proteomes:UP000186837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bard {ECO:0000313|EMBL:OJZ63958.1,
RC   ECO:0000313|Proteomes:UP000186837};
RA   Greninger A.L., Fang F., Jerome K.R.;
RT   "Genome sequences of unsequenced Mycobacteria.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PEG55657.1, ECO:0000313|Proteomes:UP000220340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP141170001 {ECO:0000313|EMBL:PEG55657.1,
RC   ECO:0000313|Proteomes:UP000220340};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (OCT-2017) 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:OJZ63958.1}.
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DR   EMBL; MPNS01000012; OJZ63958.1; -; Genomic_DNA.
DR   EMBL; MIJD01000011; OPE55999.1; -; Genomic_DNA.
DR   EMBL; PDCR01000005; PEG55657.1; -; Genomic_DNA.
DR   RefSeq; WP_073858131.1; NZ_PDCR01000005.1.
DR   AlphaFoldDB; A0A1Q4H8U0; -.
DR   STRING; 1801.BRW64_19690; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000186837; Unassembled WGS sequence.
DR   Proteomes; UP000191039; Unassembled WGS sequence.
DR   Proteomes; UP000220340; 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: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.
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   131 AA;  13818 MW;  E214394BC96453AC CRC64;
     MSEIPSDLQY TAEHEWVRRT GEDTVRVGIT DYAQAALGDV VFVQLPDVGA AVTAGDSFGE
     VESTKSLSDL YAPVTAKVVA VNGELEGSPE LVNSDPYGEG WLVELQIEDA PAAGPLPGLL
     DADGYRGILP E
//
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