GCSH_BARHE
ID GCSH_BARHE Reviewed; 122 AA.
AC Q6G2F0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-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=BH12830;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF28057.1; -; Genomic_DNA.
DR RefSeq; WP_011181097.1; NZ_LRIJ02000001.1.
DR PDB; 3MXU; X-ray; 1.80 A; A=1-122.
DR PDBsum; 3MXU; -.
DR AlphaFoldDB; Q6G2F0; -.
DR SMR; Q6G2F0; -.
DR STRING; 283166.BH12830; -.
DR PaxDb; Q6G2F0; -.
DR PRIDE; Q6G2F0; -.
DR EnsemblBacteria; CAF28057; CAF28057; BH12830.
DR KEGG; bhe:BH12830; -.
DR eggNOG; COG0509; Bacteria.
DR OMA; YRDSHEW; -.
DR EvolutionaryTrace; Q6G2F0; -.
DR Proteomes; UP000000421; 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 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; Lipoyl.
FT CHAIN 1..122
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000302355"
FT DOMAIN 19..101
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 60
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3MXU"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:3MXU"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:3MXU"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:3MXU"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3MXU"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:3MXU"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3MXU"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:3MXU"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:3MXU"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:3MXU"
FT TURN 91..95
FT /evidence="ECO:0007829|PDB:3MXU"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:3MXU"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:3MXU"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3MXU"
SQ SEQUENCE 122 AA; 13403 MW; 2FE4925EEC5DD966 CRC64;
MSKTYFTQDH EWLSVEGQVV TVGITDYAQE QLGDLVFIDL PQNGTKLSKG DAAAVVESVK
AASDVYAPLD GEVVEINAAL AESPELVNQK AETEGWLWKM TVQDETQLER LLDEAAYKEL
IG
