GCSH_BACSU
ID GCSH_BACSU Reviewed; 127 AA.
AC O32174;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
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}; Synonyms=yusH;
GN OrderedLocusNames=BSU32800;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION AS A LIPOYL CARRIER, ROLE IN PROTEIN LIPOYLATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=21338421; DOI=10.1111/j.1365-2958.2011.07598.x;
RA Christensen Q.H., Martin N., Mansilla M.C., de Mendoza D., Cronan J.E.;
RT "A novel amidotransferase required for lipoic acid cofactor assembly in
RT Bacillus subtilis.";
RL Mol. Microbiol. 80:350-363(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 -!- 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, ECO:0000269|PubMed:21338421}.
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 -!- DISRUPTION PHENOTYPE: Strains are lipoate auxotrophs. The requirement
CC for lipoic acid can be bypassed by addition of both acetate and
CC branched-chain fatty acid (BCFA) precursors.
CC {ECO:0000269|PubMed:21338421}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000255|HAMAP-
CC Rule:MF_00272}.
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DR EMBL; AL009126; CAB15269.1; -; Genomic_DNA.
DR PIR; A70021; A70021.
DR RefSeq; NP_391159.1; NC_000964.3.
DR RefSeq; WP_003222781.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32174; -.
DR SMR; O32174; -.
DR STRING; 224308.BSU32800; -.
DR jPOST; O32174; -.
DR PaxDb; O32174; -.
DR PRIDE; O32174; -.
DR EnsemblBacteria; CAB15269; CAB15269; BSU_32800.
DR GeneID; 64305036; -.
DR GeneID; 936724; -.
DR KEGG; bsu:BSU32800; -.
DR PATRIC; fig|224308.179.peg.3554; -.
DR eggNOG; COG0509; Bacteria.
DR InParanoid; O32174; -.
DR OMA; YRDSHEW; -.
DR PhylomeDB; O32174; -.
DR BioCyc; BSUB:BSU32800-MON; -.
DR PRO; PR:O32174; -.
DR Proteomes; UP000001570; 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:0009107; P:lipoate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; IMP:UniProtKB.
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 Lipoyl; Reference proteome.
FT CHAIN 1..127
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000166205"
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 127 AA; 14254 MW; E179F9EC7DD7F222 CRC64;
MSIPKDLRYS GEHEWVKVEG EKARIGITHF AQSELGDIVF VELPEVGAEI KADEPFGSVE
SVKTVSELYA PINGTVVEVN EDLDDSPEFV NESPYEKAWM IVVEPSDASE IEKLMTAEQY
EEMTQED
