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Database: UniProt
Entry: B8DWL6_BIFA0
LinkDB: B8DWL6_BIFA0
Original site: B8DWL6_BIFA0 
ID   B8DWL6_BIFA0            Unreviewed;       136 AA.
AC   B8DWL6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
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:ACL28867.1};
GN   OrderedLocusNames=BLA_0570 {ECO:0000313|EMBL:ACL28867.1};
OS   Bifidobacterium animalis subsp. lactis (strain AD011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL28867.1, ECO:0000313|Proteomes:UP000002456};
RN   [1] {ECO:0000313|EMBL:ACL28867.1, ECO:0000313|Proteomes:UP000002456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD011 {ECO:0000313|EMBL:ACL28867.1,
RC   ECO:0000313|Proteomes:UP000002456};
RX   PubMed=19011029; DOI=10.1128/JB.01515-08;
RA   Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA   Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT   "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT   lactis AD011.";
RL   J. Bacteriol. 191:678-679(2009).
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; CP001213; ACL28867.1; -; Genomic_DNA.
DR   RefSeq; WP_004218302.1; NC_011835.1.
DR   AlphaFoldDB; B8DWL6; -.
DR   STRING; 442563.BLA_0570; -.
DR   GeneID; 66533698; -.
DR   KEGG; bla:BLA_0570; -.
DR   HOGENOM; CLU_097408_2_2_11; -.
DR   Proteomes; UP000002456; 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:UP000002456}.
FT   DOMAIN          32..114
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         73
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT                   ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   136 AA;  14936 MW;  4E17742B3C3D71A0 CRC64;
     MAEENEQGTH LDVPDFLQYS HDHVWVDESV TPAVLGITEF AANKMGDIVF VDLPEVGMRV
     EAGDELVQIE SAKAVEPMIS PVAGVVRYVN SETEDDGAVI NDDPYGEGWI VKIELDDDEP
     DLLSAGEYAK FIAQQQ
//
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