ID   K1PF_MYCPN              Reviewed;         300 AA.
AC   P75038;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Putative 1-phosphofructokinase {ECO:0000250|UniProtKB:P0AEW9};
DE            EC=2.7.1.56 {ECO:0000250|UniProtKB:P0AEW9};
DE   AltName: Full=Fructose 1-phosphate kinase {ECO:0000250|UniProtKB:P0AEW9};
DE            Short=Fru1PK {ECO:0000250|UniProtKB:P0AEW9};
GN   Name=fruK; OrderedLocusNames=MPN_079; ORFNames=MP076;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=11271496;
RX   DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA   Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA   Frank R.;
RT   "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL   Electrophoresis 21:3765-3780(2000).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC       phosphate to fructose-l,6-bisphosphate. {ECO:0000250|UniProtKB:P0AEW9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:14213, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:138881,
CC         ChEBI:CHEBI:456216; EC=2.7.1.56;
CC         Evidence={ECO:0000250|UniProtKB:P0AEW9};
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; U00089; AAB95724.1; -; Genomic_DNA.
DR   PIR; S73402; S73402.
DR   RefSeq; NP_109767.1; NC_000912.1.
DR   RefSeq; WP_010874436.1; NC_000912.1.
DR   AlphaFoldDB; P75038; -.
DR   SMR; P75038; -.
DR   IntAct; P75038; 1.
DR   STRING; 272634.MPN_079; -.
DR   EnsemblBacteria; AAB95724; AAB95724; MPN_079.
DR   KEGG; mpn:MPN_079; -.
DR   PATRIC; fig|272634.6.peg.80; -.
DR   HOGENOM; CLU_050013_1_0_14; -.
DR   OMA; GHVNMAH; -.
DR   BioCyc; MPNE272634:G1GJ3-123-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   PROSITE; PS00583; PFKB_KINASES_1; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..300
FT                   /note="Putative 1-phosphofructokinase"
FT                   /id="PRO_0000080069"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT   BINDING         214..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT   BINDING         246..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J6"
SQ   SEQUENCE   300 AA;  33588 MW;  7CC8409ECD9BD48E CRC64;
     MLNHNSKVWI VNYACAIDYY LDKHKQQRGV LTPGGKGINM AIVMALFGIK PTVLTFLGQP
     TKDLFLQLLK PYQLDLVSFP ATTQTRINVK LLDGAQTTEI NDVTPLIEEQ AVHEMIAYLK
     ANVKPNDLLV LNGRFLQRDL VKLLDVAFSL TKYVVLDVDE PQLLQLLNQR QPWLMKPNRD
     EFVAMVNANN SNVDQQELVQ LIKQFQTTQN LLMSDGAQGA YFFDQQQLLF MEAIPPQQLV
     STTGAGDTLL GVFLANLLLD KDPVGSLKVA VNYASATISK LAVVNSNDQI VLKATNYYYL