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GCSH_TREDE
ID   GCSH_TREDE              Reviewed;         122 AA.
AC   Q73M83;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; OrderedLocusNames=TDE_1626;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12143.1; -; Genomic_DNA.
DR   RefSeq; NP_972232.1; NC_002967.9.
DR   RefSeq; WP_002669223.1; NC_002967.9.
DR   AlphaFoldDB; Q73M83; -.
DR   SMR; Q73M83; -.
DR   STRING; 243275.TDE_1626; -.
DR   EnsemblBacteria; AAS12143; AAS12143; TDE_1626.
DR   GeneID; 2739735; -.
DR   KEGG; tde:TDE_1626; -.
DR   PATRIC; fig|243275.7.peg.1554; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_2_12; -.
DR   OMA; YRDSHEW; -.
DR   OrthoDB; 1773485at2; -.
DR   Proteomes; UP000008212; 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..122
FT                   /note="Glycine cleavage system H protein"
FT                   /id="PRO_1000022208"
FT   DOMAIN          22..103
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   122 AA;  13585 MW;  1E74A8412472ECC7 CRC64;
     MEIKEDVKYL ESHEWFKKEG NIGIIGISDY AQSEMGDVVF IELPEVGDEV TADKACATVE
     SVKAVFEIIS PMTGKVVEIN EELLDAPEKI NEDAFGSWFF KVELKGESSK LMDAGKYKGL
     CK
 
 
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