PHK_BRUSU
ID PHK_BRUSU Reviewed; 789 AA.
AC Q8FWR0; G0KCC4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Probable phosphoketolase {ECO:0000255|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000255|HAMAP-Rule:MF_01403};
GN Name=xfp; OrderedLocusNames=BRA0385, BS1330_II0382;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01403};
CC -!- SIMILARITY: Belongs to the XFP family. {ECO:0000255|HAMAP-
CC Rule:MF_01403}.
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DR EMBL; AE014292; AAN33583.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM19862.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FWR0; -.
DR SMR; Q8FWR0; -.
DR EnsemblBacteria; AEM19862; AEM19862; BS1330_II0382.
DR KEGG; bms:BRA0385; -.
DR KEGG; bsi:BS1330_II0382; -.
DR HOGENOM; CLU_013954_2_0_5; -.
DR OMA; LSTMDHC; -.
DR PRO; PR:Q8FWR0; -.
DR Proteomes; UP000007104; Chromosome II.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.920; -; 1.
DR HAMAP; MF_01403; Phosphoketolase; 1.
DR InterPro; IPR023962; Phosphoketolase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005593; Xul5P/Fru6P_PKetolase.
DR InterPro; IPR018969; Xul5P/Fru6P_PKetolase_C.
DR InterPro; IPR019790; Xul5P/Fru6P_PKetolase_CS.
DR InterPro; IPR018970; Xul5P/Fru6P_PKetolase_N.
DR InterPro; IPR019789; Xul5P/Fru6P_PKetolase_ThDP_BS.
DR PANTHER; PTHR31273; PTHR31273; 1.
DR Pfam; PF03894; XFP; 1.
DR Pfam; PF09363; XFP_C; 1.
DR Pfam; PF09364; XFP_N; 1.
DR PIRSF; PIRSF017245; Phosphoketolase; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Lyase; Thiamine pyrophosphate.
FT CHAIN 1..789
FT /note="Probable phosphoketolase"
FT /id="PRO_0000193873"
SQ SEQUENCE 789 AA; 89267 MW; 6A1D30E5C84580D6 CRC64;
MPAKGPLTPQ QLSLINRYWR AANYLSVGQI YLMKNPLLRE PLQPEHIKPR LLGHWGTTPG
LNFIYAHLNR IIQQRNANVI YICGPGHGGP GMVANTYLEG TYSEIYPAIS EDEAGMERLF
RQFSFPGGIP SHAAPETPGS IHEGGELGYA LVHAYGAAFD NPDLVVACVV GDGEAETGAL
ATSWHSNKFL NPARDGAVLP ILHLNGYKIA NPTVLARLSD DDLDNLFRGY GYEPFFVEGS
EPADMHQKMA ATLDTIFQRI QDIKKNADVH SPERPRWPMI ILRSPKGWTG PKTVDGLVVE
NYWRAHQVPV ANCRENDAHR KILEDWMKSY DPSDLFDEKG ALKPELRALA PKGEARIGAN
PHANGGLLRK ELHMPDFRQY AVNVTEPGAI EAQSTKILGD FLRDVMKLNE TEKNFRIFGP
DETASNRLGS VLEATNRVWM AETLDMDDHL AADGRVMEVL SEHLCQGWLE GYLLSGRHGF
FSCYEAFIHI IDSMFNQHAK WLQVARELEW RKPISSLNYL LTSHVWRQDH NGFSHQDPGF
VDLVANKSAD IVRVYFPPDA NTLLWVGDHC LKTWNRVNVI VAGKQPEPQW LTMAEAEKHC
EAGLGIWEWA GTEDGLEPDI VMACAGDVPT METLAAVDLL RQSLPHLRIR VVNVVDLMVL
QSPHQHPHGI SDEEFDRMFT TNRPVIFAYH GYPYLIHRLV YKRTNHSNFH VRGFIEQGTT
TTPFDMTVLN ELDRFHLAME AVERLPLGES VAKPLIDNFT EKLALHKDYI RQHGEDMPEI
RDWKWTWPR