ID D9QM98_BRESC Unreviewed; 121 AA.
AC D9QM98;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN OrderedLocusNames=Bresu_2717 {ECO:0000313|EMBL:ADL02024.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL02024.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP002102; ADL02024.1; -; Genomic_DNA.
DR RefSeq; WP_013270125.1; NC_014375.1.
DR AlphaFoldDB; D9QM98; -.
DR STRING; 633149.Bresu_2717; -.
DR KEGG; bsb:Bresu_2717; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_0_5; -.
DR InParanoid; D9QM98; -.
DR OrthoDB; 9796712at2; -.
DR BioCyc; BSUB633149:G1GM8-2722-MONOMER; -.
DR Proteomes; UP000002696; 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:SF3; GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL; 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:UP000002696}.
FT DOMAIN 16..98
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 57
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 121 AA; 12656 MW; 1709BDD33CEC9656 CRC64;
MHFTKDHEWV RLDGDVATVG ITKHAAEQLG DVVFVETPEA GKTFGKGDSF AVVESVKAAS
DVYAPVSGDV VEGNAALAGA PETVNADPEG EGWFAKIKVS DASQVDGLMD RAAYDAFLAT
L
//