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Database: UniProt/TrEMBL
Entry: Q3A4F3_PELCD
LinkDB: Q3A4F3_PELCD
Original site: Q3A4F3_PELCD 
ID   Q3A4F3_PELCD            Unreviewed;       363 AA.
AC   Q3A4F3;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   29-APR-2015, entry version 72.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01976};
GN   Name=pfk-1 {ECO:0000313|EMBL:ABA88754.1};
GN   Synonyms=pfkA {ECO:0000256|HAMAP-Rule:MF_01976};
GN   OrderedLocusNames=Pcar_1508 {ECO:0000313|EMBL:ABA88754.1};
OS   Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Pelobacteraceae; Pelobacter.
OX   NCBI_TaxID=338963 {ECO:0000313|EMBL:ABA88754.1, ECO:0000313|Proteomes:UP000002534};
RN   [1] {ECO:0000313|Proteomes:UP000002534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / Gra Bd 1 {ECO:0000313|Proteomes:UP000002534};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01976};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01976, ECO:0000256|SAAS:SAAS00041065}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976,
CC       ECO:0000256|SAAS:SAAS00054613}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. Mixed-substrate PFK group III subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01976}.
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DR   EMBL; CP000142; ABA88754.1; -; Genomic_DNA.
DR   RefSeq; YP_006717234.1; NC_007498.2.
DR   ProteinModelPortal; Q3A4F3; -.
DR   STRING; 338963.Pcar_1508; -.
DR   EnsemblBacteria; ABA88754; ABA88754; Pcar_1508.
DR   KEGG; pca:Pcar_1508; -.
DR   PATRIC; 22889172; VBIPelCar86875_1649.
DR   eggNOG; COG0205; -.
DR   HOGENOM; HOG000248869; -.
DR   KO; K00850; -.
DR   OMA; RGLYNND; -.
DR   OrthoDB; EOG644ZRM; -.
DR   BioCyc; PCAR338963:GKDU-1673-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000002534; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
DR   TIGRFAMs; TIGR02483; PFK_mixed; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|RuleBase:RU004092};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002534};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041050};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041074};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|RuleBase:RU004092};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041077};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00041029};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|RuleBase:RU004092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002534};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|RuleBase:RU004092}.
FT   NP_BIND      76     77       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   NP_BIND     117    120       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   REGION      140    142       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      184    186       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      287    290       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    142    142       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   METAL       118    118       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      12     12       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     177    177       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     237    237       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   BINDING     281    281       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   SITE        119    119       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   363 AA;  38904 MW;  40DF99FCD29A3473 CRC64;
     MSRCIALLNG GGDCPGLNGV IRGVVRAAVL QRGWRVLGVE DGFDGLVEGP RCRELDLKSV
     CGILPRGGTI LGTSNRGNPF RYPVANENGD VILKDVSRQV VDHFQKLGAD ALVAVGGDGT
     LKIARRLSDL GIPVVGVPKT IDNDLQETDV TFGYNTAVGI VTEALDRLQT TAESHHRVMV
     VEVMGRDAGW IALEAGIAGS AEVILLPEIP FDLDLVCDHI MDRRARGSRF SIIVVAEGAF
     PKGGRKIVQA SADQTHGLER LGGIGHYVAA EIGRRKGLET RVVVLGHVQR GGTPSPFDRI
     LASRFGVRAV QLIEREEYGH MVALRGRDVV SVPIEQAVDG QNLVDPDANL VWTAEQLGIM
     LGR
//
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