GCSH_MYCTU
ID GCSH_MYCTU Reviewed; 134 AA.
AC P9WN55; L0T7T4; Q50607;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=Rv1826;
GN ORFNames=MTCY1A11.17c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44592.1; -; Genomic_DNA.
DR PIR; C70721; C70721.
DR RefSeq; NP_216342.1; NC_000962.3.
DR RefSeq; WP_003899040.1; NZ_NVQJ01000013.1.
DR PDB; 3HGB; X-ray; 1.75 A; A=1-134.
DR PDB; 3IFT; X-ray; 2.00 A; A=2-134.
DR PDB; 5EXK; X-ray; 1.86 A; B/D/F/H/J/L=62-69.
DR PDBsum; 3HGB; -.
DR PDBsum; 3IFT; -.
DR PDBsum; 5EXK; -.
DR AlphaFoldDB; P9WN55; -.
DR SMR; P9WN55; -.
DR STRING; 83332.Rv1826; -.
DR iPTMnet; P9WN55; -.
DR PaxDb; P9WN55; -.
DR DNASU; 885720; -.
DR GeneID; 885720; -.
DR KEGG; mtu:Rv1826; -.
DR TubercuList; Rv1826; -.
DR eggNOG; COG0509; Bacteria.
DR OMA; YRDSHEW; -.
DR PhylomeDB; P9WN55; -.
DR Proteomes; UP000001584; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Lipoyl; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..134
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000166228"
FT DOMAIN 24..106
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MOD_RES 65
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:3HGB"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3HGB"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:3HGB"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3HGB"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:3HGB"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3HGB"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:3HGB"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3HGB"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3HGB"
FT TURN 96..100
FT /evidence="ECO:0007829|PDB:3HGB"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3HGB"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:3HGB"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:3HGB"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:3HGB"
SQ SEQUENCE 134 AA; 14238 MW; 06D2A553236E7668 CRC64;
MSDIPSDLHY TAEHEWIRRS GDDTVRVGIT DYAQSALGDV VFVQLPVIGT AVTAGETFGE
VESTKSVSDL YAPISGKVSE VNSDLDGTPQ LVNSDPYGAG WLLDIQVDSS DVAALESALT
TLLDAEAYRG TLTE
