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Database: UniProt
Entry: Q1GDZ2_RUEST
LinkDB: Q1GDZ2_RUEST
Original site: Q1GDZ2_RUEST 
ID   Q1GDZ2_RUEST            Unreviewed;       119 AA.
AC   Q1GDZ2;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272};
GN   OrderedLocusNames=TM1040_2392 {ECO:0000313|EMBL:ABF65124.1};
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF65124.1, ECO:0000313|Proteomes:UP000000636};
RN   [1] {ECO:0000313|Proteomes:UP000000636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABF65124.1, ECO:0000313|Proteomes:UP000000636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040 {ECO:0000313|EMBL:ABF65124.1,
RC   ECO:0000313|Proteomes:UP000000636};
RX   PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA   Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA   Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA   Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA   Saunders E., Buchan A.;
RT   "Ecological genomics of marine Roseobacters.";
RL   Appl. Environ. Microbiol. 73:4559-4569(2007).
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; CP000377; ABF65124.1; -; Genomic_DNA.
DR   RefSeq; WP_011539712.1; NC_008044.1.
DR   AlphaFoldDB; Q1GDZ2; -.
DR   STRING; 292414.TM1040_2392; -.
DR   KEGG; sit:TM1040_2392; -.
DR   eggNOG; COG0509; Bacteria.
DR   HOGENOM; CLU_097408_2_0_5; -.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000000636; 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:UP000000636}.
FT   DOMAIN          16..98
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         57
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT                   ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   119 AA;  13064 MW;  800E1B20CFADB56E CRC64;
     MKYTEEHEWL QVEGDVVTVG ITSHAAEQLG DVVFVELPEV GSEVSKDDEI VVIESVKAAS
     DILAPLDGEV VEVNEAIVDA PSKVNEDPEG EAWFFKLKVS DMSPMDDYMD EAGYKDFIG
//
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