GCSH_ECOLI
ID GCSH_ECOLI Reviewed; 129 AA.
AC P0A6T9; P23884; Q2M9T7; Q8Z3W9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272, ECO:0000303|PubMed:8375392};
GN OrderedLocusNames=b2904, JW2872;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1802033; DOI=10.3109/10425179109008434;
RA Stauffer L.T., Steiert P.S., Steiert J.G., Stauffer G.V.;
RT "An Escherichia coli protein with homology to the H-protein of the glycine
RT cleavage enzyme complex from pea and chicken liver.";
RL DNA Seq. 2:13-17(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8375392; DOI=10.1111/j.1432-1033.1993.tb18172.x;
RA Okamura-Ikeda K., Ohmura Y., Fujiwara K., Motokawa Y.;
RT "Cloning and nucleotide sequence of the gcv operon encoding the Escherichia
RT coli glycine-cleavage system.";
RL Eur. J. Biochem. 216:539-548(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RC STRAIN=K12;
RX PubMed=8219277; DOI=10.3109/10425179309020835;
RA Stauffer L.T., Ghrist A., Stauffer G.V.;
RT "The Escherichia coli gcvT gene encoding the T-protein of the glycine
RT cleavage enzyme system.";
RL DNA Seq. 3:339-346(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-129.
RX PubMed=8181752; DOI=10.1016/0378-1119(94)90349-2;
RA Stauffer L.T., Fogarty S.J., Stauffer G.V.;
RT "Characterization of the Escherichia coli gcv operon.";
RL Gene 142:17-22(1994).
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 ECO:0000269|PubMed:8375392}.
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 ECO:0000269|PubMed:8375392}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000255|HAMAP-
CC Rule:MF_00272}.
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DR EMBL; M57690; AAA68887.1; -; Genomic_DNA.
DR EMBL; X73958; CAA52145.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69072.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75942.1; -; Genomic_DNA.
DR EMBL; M97263; AAC36844.1; -; Unassigned_DNA.
DR EMBL; L20872; AAA23866.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76969.1; -; Genomic_DNA.
DR PIR; A56623; A56623.
DR RefSeq; NP_417380.1; NC_000913.3.
DR RefSeq; WP_001295377.1; NZ_STEB01000001.1.
DR PDB; 3A7A; X-ray; 3.10 A; B/D=2-129.
DR PDB; 3A7L; X-ray; 1.30 A; A=2-129.
DR PDB; 3A8I; X-ray; 1.99 A; E/F=1-129.
DR PDB; 3A8J; X-ray; 1.98 A; E/F=1-129.
DR PDB; 3A8K; X-ray; 1.95 A; E/F=1-129.
DR PDB; 3AB9; X-ray; 1.65 A; A=1-129.
DR PDBsum; 3A7A; -.
DR PDBsum; 3A7L; -.
DR PDBsum; 3A8I; -.
DR PDBsum; 3A8J; -.
DR PDBsum; 3A8K; -.
DR PDBsum; 3AB9; -.
DR AlphaFoldDB; P0A6T9; -.
DR SMR; P0A6T9; -.
DR BioGRID; 4261019; 43.
DR BioGRID; 851715; 2.
DR ComplexPortal; CPX-3949; Glycine cleavage system complex.
DR IntAct; P0A6T9; 2.
DR STRING; 511145.b2904; -.
DR jPOST; P0A6T9; -.
DR PaxDb; P0A6T9; -.
DR PRIDE; P0A6T9; -.
DR EnsemblBacteria; AAC75942; AAC75942; b2904.
DR EnsemblBacteria; BAE76969; BAE76969; BAE76969.
DR GeneID; 67415210; -.
DR GeneID; 947393; -.
DR KEGG; ecj:JW2872; -.
DR KEGG; eco:b2904; -.
DR PATRIC; fig|1411691.4.peg.3828; -.
DR EchoBASE; EB0366; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_1_6; -.
DR InParanoid; P0A6T9; -.
DR OMA; YRDSHEW; -.
DR PhylomeDB; P0A6T9; -.
DR BioCyc; EcoCyc:GCVH-MON; -.
DR BioCyc; MetaCyc:GCVH-MON; -.
DR BRENDA; 1.4.1.27; 2026.
DR EvolutionaryTrace; P0A6T9; -.
DR PRO; PR:P0A6T9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005960; C:glycine cleavage complex; IC:ComplexPortal.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IC:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lipoyl; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8375392"
FT CHAIN 2..129
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000166218"
FT DOMAIN 24..106
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
FT MOD_RES 65
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:3A8K"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:3A7L"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3A7L"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:3A7L"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3A7L"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:3A7L"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3A7L"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:3A7L"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:3A7L"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3A7L"
FT TURN 96..100
FT /evidence="ECO:0007829|PDB:3A7L"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:3A7L"
FT HELIX 110..115
FT /evidence="ECO:0007829|PDB:3A7L"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3A8I"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:3A7L"
SQ SEQUENCE 129 AA; 13811 MW; 79748C818BD1325F CRC64;
MSNVPAELKY SKEHEWLRKE ADGTYTVGIT EHAQELLGDM VFVDLPEVGA TVSAGDDCAV
AESVKAASDI YAPVSGEIVA VNDALSDSPE LVNSEPYAGG WIFKIKASDE SELESLLDAT
AYEALLEDE
