(data stored in ACNUC1104 zone)

SWISSPROT: A4F718_SACEN

ID   A4F718_SACEN            Unreviewed;       131 AA.
AC   A4F718;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 83.
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:CAL99842.1};
GN   OrderedLocusNames=SACE_0494 {ECO:0000313|EMBL:CAL99842.1};
GN   ORFNames=A8924_0893 {ECO:0000313|EMBL:PFG93643.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99842.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99842.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99842.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93643.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93643.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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, ECO:0000256|SAAS:SAAS00846624}.
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       ECO:0000256|SAAS:SAAS00846613}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00272, ECO:0000256|SAAS:SAAS00846615}.
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DR   EMBL; AM420293; CAL99842.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93643.1; -; Genomic_DNA.
DR   RefSeq; WP_009951290.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0494; -.
DR   EnsemblBacteria; CAL99842; CAL99842; SACE_0494.
DR   KEGG; sen:SACE_0494; -.
DR   eggNOG; ENOG4105KE9; Bacteria.
DR   eggNOG; COG0509; LUCA.
DR   HOGENOM; HOG000239392; -.
DR   KO; K02437; -.
DR   OMA; NAWIAVL; -.
DR   OrthoDB; 1773485at2; -.
DR   BioCyc; SERY405948:SACE_RS02435-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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;
DR   PRODOM; A4F718.
DR   SWISS-2DPAGE; A4F718.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Lipoyl {ECO:0000256|HAMAP-Rule:MF_00272,
KW   ECO:0000256|PIRSR:PIRSR617453-50, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN       24    106       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   MOD_RES      65     65       N6-lipoyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00272, ECO:0000256|PIRSR:PIRSR617453-
FT                                50}.
SQ   SEQUENCE   131 AA;  14253 MW;  58C719CE7C2E3EFD CRC64;
     MVNIPQGLKY TQDHEWVEAR SGDTVRIGIT DHAQRELGDI VFVEMPEVGR RVSGAEALGS
     VESVKAVAEF FAPLGGEVVE VNSQVSDEPE LVNTDPYGDG WIVAIKVADR SELDSLMSAE
     QYGEFVAEAN E
//

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