(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NWJ7_YERPA

ID   A0A0E1NWJ7_YERPA        Unreviewed;       284 AA.
AC   A0A0E1NWJ7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 22.
DE   SubName: Full=Tagatose-bisphosphate aldolase catalytic subunit {ECO:0000313|EMBL:ABG12394.1};
GN   OrderedLocusNames=YPA_0426 {ECO:0000313|EMBL:ABG12394.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12394.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12394.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12394.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG12394.1; -; Genomic_DNA.
DR   RefSeq; WP_002209888.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12394; ABG12394; YPA_0426.
DR   EnsemblBacteria; AJJ79663; AJJ79663; CH58_3274.
DR   KEGG; ypa:YPA_0426; -.
DR   PATRIC; fig|360102.15.peg.3440; -.
DR   KO; K08302; -.
DR   OMA; VGGMEDG; -.
DR   BioCyc; YPES360102:GHZU-447-MONOMER; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0009025; F:tagatose-bisphosphate aldolase 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   InterPro; IPR011288; TagBP_ald_KbaY/GatY.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
DR   TIGRFAMs; TIGR01858; tag_bisphos_ald; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NWJ7.
DR   SWISS-2DPAGE; A0A0E1NWJ7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Lyase {ECO:0000256|SAAS:SAAS00132197};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3,
KW   ECO:0000256|SAAS:SAAS00132199};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001359-3, ECO:0000256|SAAS:SAAS00132210}.
FT   REGION      209    211       Dihydroxyacetone phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR001359-2}.
FT   REGION      230    233       Dihydroxyacetone phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR001359-2}.
FT   ACT_SITE     82     82       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001359-1}.
FT   METAL        83     83       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   METAL       104    104       Zinc 2. {ECO:0000256|PIRSR:PIRSR001359-
FT                                3}.
FT   METAL       134    134       Zinc 2. {ECO:0000256|PIRSR:PIRSR001359-
FT                                3}.
FT   METAL       180    180       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   METAL       208    208       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   BINDING     181    181       Dihydroxyacetone phosphate; via amide
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR001359-
FT                                2}.
SQ   SEQUENCE   284 AA;  31090 MW;  CB323CB1361A620F CRC64;
     MFLVSSREML RQAQIGGYAI PAFNIHNLET IQAVVETAAE MASPVILAGT PSTFSYAGTE
     YLVQICQQAA RHYRMPFALH LDHHESYDDI TQKVAAGIKS IMIDGSHFNF EQNIALTRQV
     VEYCHRWDGT VEAELGRLGG QEDDLTVDEK DALYTDPGSA AHFIQATGID SLAIAIGTAH
     GMYKEAPSLD FDRLALIRRN TDIPLVLHGG SGIPDEDVRR CIELGISKVN VGTELKIAFS
     GALKAYFLEN KGANDPRHYM VPAKAAMKKV IQDKINVCGS AGKR
//

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