SWISSPROT: A0A0F6BIS9_GEOS0

ID   A0A0F6BIS9_GEOS0        Unreviewed;       127 AA.
AC   A0A0F6BIS9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 24.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
DE   AltName: Full=Octanoyl/lipoyl carrier protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN   OrderedLocusNames=GY4MC1_0498 {ECO:0000313|EMBL:ADP73330.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73330.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73330.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73330.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is also involved in protein lipoylation via its role as
CC       an octanoyl/lipoyl carrier protein intermediate.
CC       {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The H protein shuttles the methylamine group of glycine
CC       from the P protein to the T protein. {ECO:0000256|HAMAP-
CC       Rule:MF_00272, ECO:0000256|SAAS:SAAS00846624}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00272};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000256|HAMAP-
CC       Rule:MF_00272};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H. {ECO:0000256|HAMAP-Rule:MF_00272,
CC       ECO:0000256|SAAS:SAAS00846613}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00272, ECO:0000256|SAAS:SAAS00846615}.
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DR   EMBL; CP002293; ADP73330.1; -; Genomic_DNA.
DR   RefSeq; WP_003248242.1; NC_014650.1.
DR   EnsemblBacteria; ADP73330; ADP73330; GY4MC1_0498.
DR   GeneID; 29236851; -.
DR   KEGG; gmc:GY4MC1_0498; -.
DR   KO; K02437; -.
DR   OMA; YRDSHEW; -.
DR   OrthoDB; 1773485at2; -.
DR   BioCyc; GSP581103:G1GOQ-549-MONOMER; -.
DR   Proteomes; UP000002034; 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;
DR   PRODOM; A0A0F6BIS9.
DR   SWISS-2DPAGE; A0A0F6BIS9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Lipoyl {ECO:0000256|HAMAP-Rule:MF_00272,
KW   ECO:0000256|PIRSR:PIRSR617453-50, ECO:0000256|SAAS:SAAS00065550}.
FT   DOMAIN       22    104       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   MOD_RES      63     63       N6-lipoyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00272, ECO:0000256|PIRSR:PIRSR617453-
FT                                50}.
SQ   SEQUENCE   127 AA;  14253 MW;  B7CD4FA71C7DB0D2 CRC64;
     MNTPKELRYS EEHEWVRVEG DKVRIGITDF AQSELGDIVF VELPEVGTEI TANEPFGSVE
     SVKTVSELYA PISGKVVEVN EALNDNPEYV NESPYEKAWM IVVEPSDISE IDNLLTAEQY
     EAMVKEG
//