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Database: UniProt
Entry: A0A2K9PP96_9FLAO
LinkDB: A0A2K9PP96_9FLAO
Original site: A0A2K9PP96_9FLAO 
ID   A0A2K9PP96_9FLAO        Unreviewed;       126 AA.
AC   A0A2K9PP96;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
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:AUP78893.1};
GN   ORFNames=C1H87_09335 {ECO:0000313|EMBL:AUP78893.1};
OS   Flavivirga eckloniae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavivirga.
OX   NCBI_TaxID=1803846 {ECO:0000313|EMBL:AUP78893.1, ECO:0000313|Proteomes:UP000235826};
RN   [1] {ECO:0000313|EMBL:AUP78893.1, ECO:0000313|Proteomes:UP000235826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ECD14 {ECO:0000313|EMBL:AUP78893.1,
RC   ECO:0000313|Proteomes:UP000235826};
RA   Lee J.H., Baik K.S., Seong C.N.;
RT   "Complete genome sequence of Flavivirga eckloniae ECD14 isolated from
RT   seaweed Ecklonia cava.";
RL   Submitted (JAN-2018) 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; CP025791; AUP78893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K9PP96; -.
DR   KEGG; fek:C1H87_09335; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000235826; 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:UP000235826}.
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;  13880 MW;  5B7BB6F50EE29FD3 CRC64;
     MNIPSELKYT KDHEWIKIEG DIATIGITDF AQGELGDIVY VEVETVDETL DAEEVFGTVE
     AVKTVSDLFL PLSGEIIEFN ETLEDEPEKV NSDPYGDGWM IKVKCSDLSQ ADGLMSADDY
     KALIGA
//
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