(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKH3_PSEAB

ID   A0A0H2ZKH3_PSEAB        Unreviewed;       354 AA.
AC   A0A0H2ZKH3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 14.
DE   SubName: Full=Fructose-1,6-bisphosphate aldolase {ECO:0000313|EMBL:ABJ15518.1};
GN   Name=fda {ECO:0000313|EMBL:ABJ15518.1};
GN   OrderedLocusNames=PA14_07230 {ECO:0000313|EMBL:ABJ15518.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15518.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15518.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15518.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ15518.1; -; Genomic_DNA.
DR   RefSeq; WP_003084964.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZKH3; -.
DR   SMR; A0A0H2ZKH3; -.
DR   EnsemblBacteria; ABJ15518; ABJ15518; PA14_07230.
DR   KEGG; pau:PA14_07230; -.
DR   KO; K01624; -.
DR   OMA; ELCKDCI; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic 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; IPR006412; Fruct_bisP_Calv.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
DR   TIGRFAMs; TIGR01521; FruBisAldo_II_B; 1.
DR   PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZKH3.
DR   SWISS-2DPAGE; A0A0H2ZKH3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Lyase {ECO:0000256|SAAS:SAAS00132197};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00132199};
KW   Zinc {ECO:0000256|SAAS:SAAS00132210}.
FT   REGION      233    235       Dihydroxyacetone phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR001359-2}.
FT   REGION      275    278       Dihydroxyacetone phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR001359-2}.
FT   ACT_SITE     83     83       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001359-1}.
FT   BINDING     199    199       Dihydroxyacetone phosphate; via amide
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR001359-
FT                                2}.
SQ   SEQUENCE   354 AA;  38574 MW;  08864F52A39FC9C7 CRC64;
     MALISMRQML DHAAEFGYGV PAFNVNNLEQ MRAIMEAADK TDSPVIVQAS AGARKYAGAP
     FLRHLILAAI EEFPHIPVVM HQDHGTSPDV CQRSIQLGFS SVMMDGSLRE DGKTPADYDY
     NVRVTQQTVA FAHACGVSVE GELGCLGSLE TGMAGEEDGV GAEGVLDHSQ LLTDPEEAAD
     FVKKTKVDAL AIAIGTSHGA YKFTKPPTGD TLSIQRIKEI HARIPDTHLV MHGSSSVPQD
     WLAIINEYGG EIKETYGVPV EEIVEGIKYG VRKVNIDTDL RLASTGAIRR FLAQNPSEFD
     PRKYFSKTVE AMRDICIARY EAFGTAGNAS KIKPISLEGM FQRYARGELD PKVN
//

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