ID GCSH_RHORT Reviewed; 126 AA.
AC Q2RPV0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=Rru_A3050;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(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: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; CP000230; ABC23845.1; -; Genomic_DNA.
DR RefSeq; WP_011390798.1; NC_007643.1.
DR RefSeq; YP_428132.1; NC_007643.1.
DR AlphaFoldDB; Q2RPV0; -.
DR SMR; Q2RPV0; -.
DR STRING; 269796.Rru_A3050; -.
DR EnsemblBacteria; ABC23845; ABC23845; Rru_A3050.
DR KEGG; rru:Rru_A3050; -.
DR PATRIC; fig|269796.9.peg.3160; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_0_5; -.
DR PhylomeDB; Q2RPV0; -.
DR Proteomes; UP000001929; 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; Reference proteome.
FT CHAIN 1..126
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000302425"
FT DOMAIN 20..102
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 61
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ SEQUENCE 126 AA; 13702 MW; A6C6CE8315550119 CRC64;
MSKLYFTEDH EWVSVDDDGI GTIGITDYAQ KQLGDVVFVE LPEIGREIER GGDAAVVESV
KAASEVYSPV SGEVVEANDS LPEAPGQVNT DALGDGWFFK VRLSEPAELD ELMDQEAYDA
FVGELD
//
