ID J6HKQ6_9FIRM Unreviewed; 123 AA.
AC J6HKQ6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:EJU23108.1};
GN ORFNames=HMPREF1152_1852 {ECO:0000313|EMBL:EJU23108.1};
OS Mogibacterium sp. CM50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU23108.1, ECO:0000313|Proteomes:UP000003142};
RN [1] {ECO:0000313|EMBL:EJU23108.1, ECO:0000313|Proteomes:UP000003142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM50 {ECO:0000313|EMBL:EJU23108.1,
RC ECO:0000313|Proteomes:UP000003142};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU23108.1}.
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DR EMBL; ALNL01000012; EJU23108.1; -; Genomic_DNA.
DR RefSeq; WP_009643439.1; NZ_ALNL01000012.1.
DR AlphaFoldDB; J6HKQ6; -.
DR STRING; 936375.HMPREF1152_1852; -.
DR PATRIC; fig|936375.3.peg.427; -.
DR eggNOG; COG0509; Bacteria.
DR OrthoDB; 9796712at2; -.
DR Proteomes; UP000003142; 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:UP000003142}.
FT DOMAIN 19..100
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 60
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 123 AA; 13651 MW; 14C9B4214C51F754 CRC64;
MADLKYSKSH EWVMEEGDLY VIGISDYAQH SLGDIVFINL PEVDDEVTVG DAFGDIESVK
AVSDVLSPVT GIVAEINEEL FDAPESINED PYGAWLIKVK DVTETEELLS SDEYDEFVES
EEA
//
