ID F8GEQ1_NITSI Unreviewed; 789 AA.
AC F8GEQ1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN OrderedLocusNames=Nit79A3_0036 {ECO:0000313|EMBL:AEI99944.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEI99944.1};
RN [1] {ECO:0000313|EMBL:AEI99944.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEI99944.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|HAMAP-Rule:MF_01403};
CC -!- SIMILARITY: Belongs to the XFP family. {ECO:0000256|ARBA:ARBA00005623,
CC ECO:0000256|HAMAP-Rule:MF_01403}.
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DR EMBL; CP002876; AEI99944.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GEQ1; -.
DR STRING; 261292.Nit79A3_0036; -.
DR KEGG; nii:Nit79A3_0036; -.
DR eggNOG; COG3957; Bacteria.
DR HOGENOM; CLU_013954_2_0_4; -.
DR OrthoDB; 9768449at2; -.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02011; TPP_PK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; PHOSPHOKETOLASE-RELATED; 1.
DR PANTHER; PTHR31273:SF0; PHOSPHOKETOLASE-RELATED; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01403};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01403}.
FT DOMAIN 9..368
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 583..784
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 789 AA; 88821 MW; 4B727E01B5CBD2A5 CRC64;
MKKNTKLLSP ELLHKMDAYW RAANYLSVGQ IYLYDNPLLK QPLKLAHIKP RLLGHWGTTP
GLNFIYVHLN RIIKEHDLNV IYITGPGHGG PGLVANTYLE GTYSEVYPNI SQDEDGMQRL
FKQFSFPGGI PSHVAPETPG SIHEGGELGY SLSHAFGAAF DNPGLLVACV VGDGEAETGP
LATSWHSNKF LNPVHDGAVL PILHLNGYKI AGPTVLARIP CDELEALFRG YGYTPYFIEG
DDPLEMHQRM AATLDAVIAN IQSIQRDART HGFTKRPHWP MIILRSPKGW TGPKVVDGKP
TEGTFRSHQV PMGDMSQPGH VKILEKWLKS YRPQELFDET GKLLAELAEL APQGARRMGA
NPHANGGMLL RDLRLPDFRD YAVKVANPGT VSAEATRTQG EFIRDVVKLN ATNFRVFSPD
ETASNRWGAV FEVTNRCSTA EIVPGDDHVA PDGRVMEMLS EHQCEGWLEG YLLTGRHGFF
SCYEAFIHII DSMFNQHAKW LKVANEIPWR RPIASLNYLL SSHVWRQDHN GFSHQDPGFI
DHVINKKAEI IRIYLPPDAN TLLSVTDHCL RSRNYVNVIV AGKQPQPQWL DMDAAIKHCT
AGIGIWEWAS NDQGEEPDVV MACAGDAPTI ETLAAVELLW KHFPELKIRV INVVDLMSLQ
PQSEHPHGLS DKDFDGLFTK DKPIIFAYHG YPWLIHRLTY RRTNHDNLHV RGYKEEGTTS
TPFDMVVMND LDRFHLVADV IDRVPQLGSR AAYVKQAIRD KLIEHKQYIN QYGEDMPEIR
NWKWKGSSV
//