ID   PFKB_THETC              Reviewed;         322 AA.
AC   D9TT10;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000305|PubMed:24599311};
DE            Short=ATP-PFK {ECO:0000305|PubMed:24599311};
DE            Short=Phosphofructokinase {ECO:0000303|PubMed:24599311};
DE            EC=2.7.1.11 {ECO:0000269|PubMed:24599311};
GN   Name=pfkB; OrderedLocusNames=Tthe_1922 {ECO:0000312|EMBL:ADL69408.1};
OS   Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS   NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS   thermosaccharolyticum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX   NCBI_TaxID=580327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC   00135 / 2032;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT   571.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=24599311; DOI=10.1007/s00253-014-5621-y;
RA   Verhaeghe T., Aerts D., Diricks M., Soetaert W., Desmet T.;
RT   "The quest for a thermostable sucrose phosphorylase reveals sucrose 6'-
RT   phosphate phosphorylase as a novel specificity.";
RL   Appl. Microbiol. Biotechnol. 98:7027-7037(2014).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-fructose 6-
CC       phosphate to fructose 1,6-bisphosphate. Together with the adjacently
CC       encoded sucrose 6'-phosphate phosphorylase, may be involved in a new
CC       pathway for the degradation of sucrose. Cannot phosphorylate D-
CC       fructose. {ECO:0000269|PubMed:24599311}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000269|PubMed:24599311};
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; CP002171; ADL69408.1; -; Genomic_DNA.
DR   RefSeq; WP_013298374.1; NC_014410.1.
DR   AlphaFoldDB; D9TT10; -.
DR   SMR; D9TT10; -.
DR   STRING; 580327.Tthe_1922; -.
DR   EnsemblBacteria; ADL69408; ADL69408; Tthe_1922.
DR   KEGG; ttm:Tthe_1922; -.
DR   eggNOG; COG0524; Bacteria.
DR   HOGENOM; CLU_027634_6_0_9; -.
DR   OMA; GAWPEYP; -.
DR   OrthoDB; 1604782at2; -.
DR   Proteomes; UP000001626; Chromosome.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   PROSITE; PS00583; PFKB_KINASES_1; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..322
FT                   /note="ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_0000442436"
FT   BINDING         201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O59128"
FT   BINDING         234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O59128"
FT   BINDING         239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O59128"
SQ   SEQUENCE   322 AA;  36535 MW;  A57BE1B25FC0ED87 CRC64;
     MFNFNDKIVF DDKKYDVLTV GEMLVDMIST DYGDDFECDT YKKYFGGSPA NIAINSKMLG
     INSIIVSSVG NDGLGKFLLK KLQEHHIEIK YVRQVDYSTS MVLVTKSKSS PTPIFYRDAD
     YHIEYSDELK YLIENTKIVH FSSWPISRNP SRSTVEILID ECKKYDVLVC YDPNYHSMIW
     ERGHDGREYI KSLIAKVDII KPSEDDAERI FGKDTPENQL KKFLDLGAKL VILTLGKDGA
     IVSNGEETIR FNTLADEVVD TTGAGDAFWS GFYSGLIKGY TLKKSLELGF AVSAYKLRYV
     GAIVDLPDID TIKSMYDLKK LR