GCSH_RHOBA
ID GCSH_RHOBA Reviewed; 132 AA.
AC Q7UNG9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=RB7586;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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:0000255|HAMAP-Rule:MF_00272}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00272};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|HAMAP-
CC Rule:MF_00272};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00272}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000255|HAMAP-
CC Rule:MF_00272}.
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DR EMBL; BX294146; CAD75450.1; -; Genomic_DNA.
DR RefSeq; NP_867903.1; NC_005027.1.
DR RefSeq; WP_011121467.1; NC_005027.1.
DR AlphaFoldDB; Q7UNG9; -.
DR SMR; Q7UNG9; -.
DR STRING; 243090.RB7586; -.
DR EnsemblBacteria; CAD75450; CAD75450; RB7586.
DR KEGG; rba:RB7586; -.
DR PATRIC; fig|243090.15.peg.3666; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_0_0; -.
DR InParanoid; Q7UNG9; -.
DR OMA; YRDSHEW; -.
DR OrthoDB; 1773485at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR CDD; cd06848; GCS_H; 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 PANTHER; PTHR11715; PTHR11715; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR00527; gcvH; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Lipoyl; Reference proteome.
FT CHAIN 1..132
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000226041"
FT DOMAIN 27..109
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 68
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ SEQUENCE 132 AA; 14514 MW; 41D017AB14594ABD CRC64;
MARDPSTLRY AETHEWVDVQ EEGGDKFATI GISAFAVEQL NDLVYMDLPE VGRTLEVGEE
FGEVESVKAV SPLYSPVAGE VVAVHTDLPD NLDNLNDDAF DFGWILKVKL SADLPETLMD
FAAYQKQCSE AG
