PFKB_MYCTO
ID PFKB_MYCTO Reviewed; 339 AA.
AC P9WID2; L0T8F1; O86352; Q7D7L4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=ATP-dependent 6-phosphofructokinase isozyme 2 {ECO:0000250|UniProtKB:P9WID3};
DE Short=ATP-PFK 2 {ECO:0000250|UniProtKB:P9WID3};
DE Short=Phosphofructokinase 2 {ECO:0000250|UniProtKB:P9WID3};
DE EC=2.7.1.11 {ECO:0000250|UniProtKB:P9WID3};
DE AltName: Full=Phosphofructokinase B {ECO:0000250|UniProtKB:P9WID3};
DE AltName: Full=Phosphohexokinase 2 {ECO:0000250|UniProtKB:P9WID3};
DE AltName: Full=Tagatose-6-phosphate kinase {ECO:0000305};
DE EC=2.7.1.144 {ECO:0000250|UniProtKB:P9WID3};
GN Name=pfkB; OrderedLocusNames=MT2088;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. Can also catalyze the phosphorylation of tagatose-6-
CC phosphate. {ECO:0000250|UniProtKB:P9WID3}.
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:0000250|UniProtKB:P9WID3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose
CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:12420, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58694, ChEBI:CHEBI:58695,
CC ChEBI:CHEBI:456216; EC=2.7.1.144;
CC Evidence={ECO:0000250|UniProtKB:P9WID3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WID3};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000250|UniProtKB:P9WID3}.
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC {ECO:0000269|PubMed:12953092}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK46367.1; -; Genomic_DNA.
DR PIR; D70942; D70942.
DR RefSeq; WP_003899139.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WID2; -.
DR SMR; P9WID2; -.
DR EnsemblBacteria; AAK46367; AAK46367; MT2088.
DR KEGG; mtc:MT2088; -.
DR PATRIC; fig|83331.31.peg.2252; -.
DR HOGENOM; CLU_050013_0_2_11; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IEA:RHEA.
DR CDD; cd01164; FruK_PfkB_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR017583; Tagatose/fructose_Pkinase.
DR Pfam; PF00294; PfkB; 1.
DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR03168; 1-PFK; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Transferase.
FT CHAIN 1..339
FT /note="ATP-dependent 6-phosphofructokinase isozyme 2"
FT /id="PRO_0000428027"
FT ACT_SITE 265
FT /evidence="ECO:0000250"
FT BINDING 22..24
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 37..39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 49..53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 100..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 233..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 35401 MW; D773E363FF73DADD CRC64;
MTEPAAWDEG KPRIITLTMN PALDITTSVD VVRPTEKMRC GAPRYDPGGG GINVARIVHV
LGGCSTALFP AGGSTGSLLM ALLGDAGVPF RVIPIAASTR ESFTVNESRT AKQYRFVLPG
PSLTVAEQEQ CLDELRGAAA SAAFVVASGS LPPGVAADYY QRVADICRRS STPLILDTSG
GGLQHISSGV FLLKASVREL RECVGSELLT EPEQLAAAHE LIDRGRAEVV VVSLGSQGAL
LATRHASHRF SSIPMTAVSG VGAGDAMVAA ITVGLSRGWS LIKSVRLGNA AGAAMLLTPG
TAACNRDDVE RFFELAAEPT EVGQDQYVWH PIVNPEASP
