ID Q5NEF5_FRATT Unreviewed; 198 AA.
AC Q5NEF5; A0A0G2RM04;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Phosphoheptose isomerase {ECO:0000313|EMBL:CAG46314.1};
DE EC=5.-.-.- {ECO:0000313|EMBL:CAG46314.1};
GN Name=lpcA {ECO:0000313|EMBL:CAG46314.1};
GN OrderedLocusNames=FTT_1681c {ECO:0000313|EMBL:CAG46314.1};
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG46314.1, ECO:0000313|Proteomes:UP000001174};
RN [1] {ECO:0000313|EMBL:CAG46314.1, ECO:0000313|Proteomes:UP000001174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
RN [2] {ECO:0007829|PDB:3TRJ}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
RX PubMed=23704901; DOI=10.1371/journal.pone.0063369;
RA Chaudhury S., Abdulhameed M.D., Singh N., Tawa G.J., D'haeseleer P.M.,
RA Zemla A.T., Navid A., Zhou C.E., Franklin M.C., Cheung J., Rudolph M.J.,
RA Love J., Graf J.F., Rozak D.A., Dankmeyer J.L., Amemiya K., Daefler S.,
RA Wallqvist A.;
RT "Rapid countermeasure discovery against Francisella tularensis based on a
RT metabolic network reconstruction.";
RL PLoS ONE 8:e63369-e63369(2013).
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DR EMBL; AJ749949; CAG46314.1; -; Genomic_DNA.
DR RefSeq; WP_003017606.1; NZ_CP010290.1.
DR RefSeq; YP_170587.1; NC_006570.2.
DR PDB; 3TRJ; X-ray; 2.80 A; A/B/C/D=1-198.
DR PDBsum; 3TRJ; -.
DR AlphaFoldDB; Q5NEF5; -.
DR SMR; Q5NEF5; -.
DR DNASU; 3191473; -.
DR EnsemblBacteria; CAG46314; CAG46314; FTT_1681c.
DR GeneID; 75264398; -.
DR KEGG; ftu:FTT_1681c; -.
DR PATRIC; fig|177416.36.peg.1055; -.
DR OrthoDB; 9810929at2; -.
DR EvolutionaryTrace; Q5NEF5; -.
DR Proteomes; UP000001174; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR CDD; cd05006; SIS_GmhA; 1.
DR InterPro; IPR035461; GmhA/DiaA.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR30390:SF6; DNAA INITIATOR-ASSOCIATING PROTEIN DIAA; 1.
DR PANTHER; PTHR30390; SEDOHEPTULOSE 7-PHOSPHATE ISOMERASE / DNAA INITIATOR-ASSOCIATING FACTOR FOR REPLICATION INITIATION; 1.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3TRJ};
KW Isomerase {ECO:0000313|EMBL:CAG46314.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001174}.
FT DOMAIN 36..198
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 198 AA; 21057 MW; DCBA00B3A0A6E813 CRC64;
MTSLDKINSY FESSIQAKIE TANALPPAIA QAAKAMVSCL ENGGKVLVCG NGSSGVIAQH
FTSKLLNHFE MERPPLPAIA LTGDVATITA VGNHYGFSQI FAKQVAALGN EDDILLVITT
SGDSENILSA VEEAHDLEMK VIALTGGSGG ALQNMYNTDD IELRVPSDNI ANIQENHFLI
VHCLCDIIDQ KLFAGLED
//
