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Database: UniProt
Entry: A9HM50_GLUDA
LinkDB: A9HM50_GLUDA
Original site: A9HM50_GLUDA 
ID   A9HM50_GLUDA            Unreviewed;       121 AA.
AC   A9HM50;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272,
GN   ECO:0000313|EMBL:CAP56259.1};
GN   OrderedLocusNames=GDI2316 {ECO:0000313|EMBL:CAP56259.1};
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS   / CIP 103539 / LMG 7603 / PAl5).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP56259.1, ECO:0000313|Proteomes:UP000001176};
RN   [1] {ECO:0000313|EMBL:CAP56259.1, ECO:0000313|Proteomes:UP000001176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 /
RC   PAl5 {ECO:0000313|Proteomes:UP000001176};
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA   Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA   Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA   Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA   Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B.,
RA   Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA   Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G.,
RA   Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C.,
RA   Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(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:0000256|HAMAP-Rule:MF_00272}.
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: P,
CC       T, L and H. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC       ECO:0000256|HAMAP-Rule:MF_00272}.
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DR   EMBL; AM889285; CAP56259.1; -; Genomic_DNA.
DR   RefSeq; WP_012226206.1; NC_011365.1.
DR   STRING; 272568.GDI2316; -.
DR   KEGG; gdi:GDI2316; -.
DR   KEGG; gdj:Gdia_0533; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_0_5; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000001176; 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   Gene3D; 2.40.50.100; -; 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   NCBIfam; TIGR00527; gcvH; 1.
DR   PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR   PANTHER; PTHR11715:SF41; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR   Pfam; PF01597; GCV_H; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|HAMAP-Rule:MF_00272};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001176}.
FT   MOD_RES         59
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272"
SQ   SEQUENCE   121 AA;  12633 MW;  65B8990064457AFC CRC64;
     MTVYYTKDHE WLRIEGDVAT VGITAHAAEE LGELVFVEAK PDGTEVAQGD SAAVVESVKA
     ASDIYAPVSG TVAGFNGALA DDPSLVNRDP EAEGWILKMR IADQGQLASL LDAAAYAALI
     A
//
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