(data stored in ACNUC7421 zone)

SWISSPROT: B1VNU1_STRGG

ID   B1VNU1_STRGG            Unreviewed;       289 AA.
AC   B1VNU1;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   SubName: Full=Putative tagatose-bisphosphate aldolase {ECO:0000313|EMBL:BAG17114.1};
GN   OrderedLocusNames=SGR_285 {ECO:0000313|EMBL:BAG17114.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17114.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17114.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS00836928};
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|SAAS:SAAS00836930}.
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DR   EMBL; AP009493; BAG17114.1; -; Genomic_DNA.
DR   RefSeq; WP_012377676.1; NC_010572.1.
DR   ProteinModelPortal; B1VNU1; -.
DR   STRING; 455632.SGR_285; -.
DR   EnsemblBacteria; BAG17114; BAG17114; SGR_285.
DR   GeneID; 6212962; -.
DR   KEGG; sgr:SGR_285; -.
DR   PATRIC; fig|455632.4.peg.264; -.
DR   eggNOG; ENOG4105D2N; Bacteria.
DR   eggNOG; COG0191; LUCA.
DR   HOGENOM; HOG000227793; -.
DR   KO; K01624; -.
DR   OMA; GENFLRH; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00947; TBP_aldolase_IIB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VNU1.
DR   SWISS-2DPAGE; B1VNU1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Lyase {ECO:0000256|SAAS:SAAS00132197};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00132199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685};
KW   Zinc {ECO:0000256|SAAS:SAAS00132210}.
FT   ACT_SITE     84     84       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001359-1}.
SQ   SEQUENCE   289 AA;  30041 MW;  21F6FE6FB661550D CRC64;
     MSIATTGDLI AEAAAQNRAV AAFNVITLEH AEAIAEGAEA AGSPVILQIS ENAVAYHRGR
     PRPLARAAAE VADQAAVPVS LHLDHVQSTE LLHRAADCGF SSAMFDAARL PYTENLAATR
     AAVLWAHERG LWLEAELGQV GGKNGEPALD AHAPGARTDP GEARSFVAAT GVDALAVAVG
     TAHAMTSRDA VIDHGLLDRL REAVPVPLVL HGSSGASDEE LARAVAGGIR KVNIGTALNI
     AMTGAIRERL ARDDRGVDPR RYLADGRDAM ARTVARMIAV LPSGRAYAA
//

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