ID   GCSH_CHRVO              Reviewed;         128 AA.
AC   Q7NSJ4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=CV_3430;
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS   12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC   9757;
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA   Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA   Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA   Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA   Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA   Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA   Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA   Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA   Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA   Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA   Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA   Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA   de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA   Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA   Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA   Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA   Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA   Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA   Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA   Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA   Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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}.
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DR   EMBL; AE016825; AAQ61093.1; -; Genomic_DNA.
DR   RefSeq; WP_011136977.1; NC_005085.1.
DR   AlphaFoldDB; Q7NSJ4; -.
DR   SMR; Q7NSJ4; -.
DR   STRING; 243365.CV_3430; -.
DR   EnsemblBacteria; AAQ61093; AAQ61093; CV_3430.
DR   KEGG; cvi:CV_3430; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_0_4; -.
DR   OMA; YRDSHEW; -.
DR   OrthoDB; 1773485at2; -.
DR   Proteomes; UP000001424; 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; 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; Reference proteome.
FT   CHAIN           1..128
FT                   /note="Glycine cleavage system H protein"
FT                   /id="PRO_0000302366"
FT   DOMAIN          24..106
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         65
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ   SEQUENCE   128 AA;  13518 MW;  4CA695187D8BF66C CRC64;
     MSNIPAELKY VDSHEWLRLE ADGSVTVGIT AHAQELLGDI VFVELPKVGA SLAKDEQAGV
     VESVKAASDV YCPIAGEVLA VNEELEGEPE LANSDPYGDG WFFKIKPANA ADLNGLMDAA
     AYAKEIGA