(data stored in SCRATCH zone)

SWISSPROT: C1ASV7_RHOOB

ID   C1ASV7_RHOOB            Unreviewed;       134 AA.
AC   C1ASV7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
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:BAH48889.1};
GN   OrderedLocusNames=ROP_06420 {ECO:0000313|EMBL:BAH48889.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48889.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48889.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48889.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The H protein shuttles the methylamine group of glycine
CC       from the P protein to the T protein. {ECO:0000256|HAMAP-
CC       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:
CC       P, T, L and H. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00272, ECO:0000256|SAAS:SAAS00846615}.
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DR   EMBL; AP011115; BAH48889.1; -; Genomic_DNA.
DR   RefSeq; WP_012687893.1; NC_012522.1.
DR   EnsemblBacteria; BAH48889; BAH48889; ROP_06420.
DR   KEGG; rop:ROP_06420; -.
DR   PATRIC; fig|632772.20.peg.702; -.
DR   eggNOG; ENOG4105KE9; Bacteria.
DR   eggNOG; COG0509; LUCA.
DR   HOGENOM; HOG000239392; -.
DR   KO; K02437; -.
DR   OMA; YRDSHEW; -.
DR   OrthoDB; 1773485at2; -.
DR   Proteomes; UP000002212; 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;
DR   PRODOM; C1ASV7.
DR   SWISS-2DPAGE; C1ASV7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Lipoyl {ECO:0000256|HAMAP-Rule:MF_00272,
KW   ECO:0000256|PIRSR:PIRSR617453-50, ECO:0000256|SAAS:SAAS00846628}.
FT   DOMAIN       26    108       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   MOD_RES      67     67       N6-lipoyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00272, ECO:0000256|PIRSR:PIRSR617453-
FT                                50}.
SQ   SEQUENCE   134 AA;  14115 MW;  75BD637C0068A22F CRC64;
     MSELEIPADR RYTAEHEWVE RTGPTTVRVG ITDFAQSQLG DVVFVQLPAV DEDVTAGESF
     GEVESTKSVS DIFAPLTAKV VAANADLDGN PELVNSAPYG QGWLVELGVD DEAALDAALA
     EMLDAAGYAD LTAG
//

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