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Database: UniProt/TrEMBL
Entry: E4WJP9_RHOE1
LinkDB: E4WJP9_RHOE1
Original site: E4WJP9_RHOE1 
ID   E4WJP9_RHOE1            Unreviewed;       343 AA.
AC   E4WJP9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   29-APR-2015, entry version 31.
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=pfkA {ECO:0000256|HAMAP-Rule:MF_01976,
GN   ECO:0000313|EMBL:CBH49157.1};
GN   OrderedLocusNames=REQ_31560 {ECO:0000313|EMBL:CBH49157.1};
OS   Rhodococcus equi (strain 103S) (Corynebacterium equi).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=685727 {ECO:0000313|EMBL:CBH49157.1, ECO:0000313|Proteomes:UP000006892};
RN   [1] {ECO:0000313|Proteomes:UP000006892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103S {ECO:0000313|Proteomes:UP000006892};
RX   PubMed=20941392; DOI=10.1371/journal.pgen.1001145;
RA   Letek M., Gonzalez P., Macarthur I., Rodriguez H., Freeman T.C.,
RA   Valero-Rello A., Blanco M., Buckley T., Cherevach I., Fahey R.,
RA   Hapeshi A., Holdstock J., Leadon D., Navas J., Ocampo A., Quail M.A.,
RA   Sanders M., Scortti M.M., Prescott J.F., Fogarty U., Meijer W.G.,
RA   Parkhill J., Bentley S.D., Vazquez-Boland J.A.;
RT   "The genome of a pathogenic rhodococcus: cooptive virulence
RT   underpinned by key gene acquisitions.";
RL   PLoS Genet. 6:E1001145-E1001145(2010).
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; FN563149; CBH49157.1; -; Genomic_DNA.
DR   RefSeq; WP_005519004.1; NC_014659.1.
DR   RefSeq; YP_004007837.1; NC_014659.1.
DR   ProteinModelPortal; E4WJP9; -.
DR   EnsemblBacteria; CBH49157; CBH49157; REQ_31560.
DR   KEGG; req:REQ_31560; -.
DR   PATRIC; 42663775; VBIRhoEqu141084_3153.
DR   HOGENOM; HOG000248869; -.
DR   KO; K00850; -.
DR   OMA; KPAEGSM; -.
DR   BioCyc; REQU685727:GHKP-3047-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000006892; 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:UP000006892};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|RuleBase:RU004092}.
FT   NP_BIND      73     74       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   NP_BIND     103    106       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   REGION      126    128       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      170    172       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      273    276       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    128    128       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   METAL       104    104       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      10     10       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     163    163       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     223    223       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   BINDING     267    267       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   SITE        105    105       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   343 AA;  37032 MW;  7A388524966ED249 CRC64;
     MRIGILTGGG DCPGLNAVIR AVVRTADSRY GSTVVGFRDG WRGLLEDRKV QMRNEDRIDR
     ILARGGTILG TARVNPQKLH DGLDRIKQTL DDNGIDVLIP IGGEGTLTAG SWLAESGVPV
     VGVPKTIDND IDCTDVTFGF DTALTIATEA IDRLHTTAES HQRVMLVEVM GRHAGWIALQ
     SGMASGAHLT LVPEVPFDVD EVCALVKKRF QRGDSHFICV VAEGAAPDPE SMTLREGGID
     EFGHKIFTGV AQQLAVEIER RIGKEVRTTV LGHVQRGGTP TPYDRVLATR FGVHATDAAH
     NGQFGQMVAL HGTNIELVPL SEATKQLKTV PVERYREAAA FFG
//
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