GCSH1_PSESM
ID GCSH1_PSESM Reviewed; 127 AA.
AC Q887L4;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Glycine cleavage system H protein 1 {ECO:0000255|HAMAP-Rule:MF_00272};
GN Name=gcvH1 {ECO:0000255|HAMAP-Rule:MF_00272}; Synonyms=gcvH-1;
GN OrderedLocusNames=PSPTO_1277;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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; AE016853; AAO54802.1; -; Genomic_DNA.
DR RefSeq; NP_791107.1; NC_004578.1.
DR RefSeq; WP_011103496.1; NC_004578.1.
DR AlphaFoldDB; Q887L4; -.
DR SMR; Q887L4; -.
DR STRING; 223283.PSPTO_1277; -.
DR EnsemblBacteria; AAO54802; AAO54802; PSPTO_1277.
DR GeneID; 1182913; -.
DR KEGG; pst:PSPTO_1277; -.
DR PATRIC; fig|223283.9.peg.1299; -.
DR eggNOG; COG0509; Bacteria.
DR HOGENOM; CLU_097408_2_0_6; -.
DR OMA; EHEWLSG; -.
DR OrthoDB; 1773485at2; -.
DR PhylomeDB; Q887L4; -.
DR Proteomes; UP000002515; 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..127
FT /note="Glycine cleavage system H protein 1"
FT /id="PRO_0000166237"
FT DOMAIN 20..101
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 60
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00272"
SQ SEQUENCE 127 AA; 13862 MW; 03C965A4D56157C0 CRC64;
MSELRFTADH EWLRAEADGS VTVGITPYAQ ESLGDVVFVQ LPELQAYAQH AEVSVVESVK
AASSINMPLD GEVVEVNAVL DATPERVNED ALGAGWFFRF IPQDAYAIHG LLDQDAYDRL
IKANAQA
