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Database: UniProt/TrEMBL
Entry: Q0AXS5_SYNWW
LinkDB: Q0AXS5_SYNWW
Original site: Q0AXS5_SYNWW 
ID   Q0AXS5_SYNWW            Unreviewed;       365 AA.
AC   Q0AXS5;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JUN-2015, entry version 71.
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   OrderedLocusNames=Swol_1170 {ECO:0000313|EMBL:ABI68479.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI68479.1, ECO:0000313|Proteomes:UP000001968};
RN   [1] {ECO:0000313|Proteomes:UP000001968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(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; CP000448; ABI68479.1; -; Genomic_DNA.
DR   RefSeq; WP_011640582.1; NC_008346.1.
DR   RefSeq; YP_753850.1; NC_008346.1.
DR   ProteinModelPortal; Q0AXS5; -.
DR   STRING; 335541.Swol_1170; -.
DR   EnsemblBacteria; ABI68479; ABI68479; Swol_1170.
DR   KEGG; swo:Swol_1170; -.
DR   PATRIC; 23857165; VBISynWol51738_1242.
DR   eggNOG; COG0205; -.
DR   HOGENOM; HOG000248869; -.
DR   KO; K00850; -.
DR   OMA; RGLYNND; -.
DR   OrthoDB; EOG644ZRM; -.
DR   BioCyc; SWOL335541:GHL1-1203-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001968; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
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-HAMAP.
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:UP000001968};
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:UP000001968};
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     116    119       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   REGION      139    141       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      183    185       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    141    141       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   METAL       117    117       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      14     14       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     176    176       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     236    236       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        118    118       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   365 AA;  39123 MW;  37E1B3E18CAD9047 CRC64;
     MKEIRHIGIL TGGGDCPGLN AVIRAISKTA INYGVEVIGF IDGFKGLVEN RYIQLDLRAV
     SGISHTGGTI LGTSNRDNPF QFFTISEGTP QHSDESDRAV ANMEHLGLDG LVVIGGDGSL
     NIADRFAEKG VPIVGVPKTI DNDLSATDVT FGFNTAVNTA SEALDRLHTT AESHHRVMVL
     EVMGRYAGWI ALHAGISGGA DVILIPEIPY NMDAVISKIT QRYRQGKNFS IIVVAEGAIP
     EDGEMVIRNL VATSHDPIRL GGIGQKVAED IGNRLQNIEV RVTVLGHLQR GGSPIPYDRI
     LSTRYGVAAV DAFMAGQFGT MVSLRGDMIA AVPIKEAIKE IRRVKPESDL VRAARAVGIS
     FGDKY
//
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