GCSH_MAGMM
ID GCSH_MAGMM Reviewed; 140 AA.
AC A0LDQ0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=Mmc1_3608;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK46093.1; -; Genomic_DNA.
DR RefSeq; WP_011715149.1; NC_008576.1.
DR AlphaFoldDB; A0LDQ0; -.
DR SMR; A0LDQ0; -.
DR STRING; 156889.Mmc1_3608; -.
DR EnsemblBacteria; ABK46093; ABK46093; Mmc1_3608.
DR KEGG; mgm:Mmc1_3608; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_0_5; -.
DR OMA; YRDSHEW; -.
DR OrthoDB; 1773485at2; -.
DR Proteomes; UP000002586; 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; 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.
PE 3: Inferred from homology;
KW Lipoyl; Reference proteome.
FT CHAIN 1..140
FT /note="Glycine cleavage system H protein"
FT /id="PRO_0000302386"
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 140 AA; 15468 MW; 87BCC8C4A7ED368D CRC64;
MSIPQELYYT KDHEWLRKEG DEVVIGITRF AADQLGDVVF VELPQVEDTL QMGGTFGVVE
SVKAASDLFS PITGQVIATN PDLAEAPELV NEDPYGKGWM LRLKPEDPAQ MDALLTAQAY
TAWLETCSSF AVRFGQNLTL