GCSH_LISIN
ID GCSH_LISIN Reviewed; 125 AA.
AC Q928L3;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
DE AltName: Full=Octanoyl/lipoyl carrier protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=lin2519;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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 -!- FUNCTION: Is also involved in protein lipoylation via its role as an
CC octanoyl/lipoyl carrier protein intermediate. {ECO:0000255|HAMAP-
CC 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; AL596172; CAC97746.1; -; Genomic_DNA.
DR PIR; AB1747; AB1747.
DR RefSeq; WP_003769150.1; NC_003212.1.
DR AlphaFoldDB; Q928L3; -.
DR SMR; Q928L3; -.
DR STRING; 272626.lin2519; -.
DR EnsemblBacteria; CAC97746; CAC97746; CAC97746.
DR GeneID; 61171681; -.
DR KEGG; lin:lin2519; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_0_9; -.
DR OMA; YRDSHEW; -.
DR OrthoDB; 1773485at2; -.
DR Proteomes; UP000002513; 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 GO; GO:0009249; P:protein lipoylation; 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 3: Inferred from homology;
KW Lipoyl.
FT CHAIN 1..125
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000166223"
FT DOMAIN 22..104
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 63
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ SEQUENCE 125 AA; 13732 MW; 94F00032FBCFA152 CRC64;
MSLPKDLLYT EEHEWVKAED GSYIIGITDF AQDQLGDIVF VELPEVGDTV TKGDSIGSIE
SVKTVSDFYA PVTGKVVAVN ETLEDEPELI NSNPYDTGWI LKLTEVEEAD VTALLSSDDY
EKGLD