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Database: UniProt/TrEMBL
Entry: D9SST4_CLOC7
LinkDB: D9SST4_CLOC7
Original site: D9SST4_CLOC7 
ID   D9SST4_CLOC7            Unreviewed;       366 AA.
AC   D9SST4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   29-APR-2015, entry version 29.
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=Clocel_2901 {ECO:0000313|EMBL:ADL52596.1};
OS   Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 /
OS   743B).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL52596.1, ECO:0000313|Proteomes:UP000002730};
RN   [1] {ECO:0000313|EMBL:ADL52596.1, ECO:0000313|Proteomes:UP000002730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC   {ECO:0000313|Proteomes:UP000002730};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium cellulovorans 743B.";
RL   Submitted (AUG-2010) 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; CP002160; ADL52596.1; -; Genomic_DNA.
DR   RefSeq; WP_010075689.1; NZ_BABR01000307.1.
DR   RefSeq; YP_003844360.1; NC_014393.1.
DR   ProteinModelPortal; D9SST4; -.
DR   EnsemblBacteria; ADL52596; ADL52596; Clocel_2901.
DR   KEGG; ccb:Clocel_2901; -.
DR   PATRIC; 41737482; VBICloCel81632203721_2512.
DR   HOGENOM; HOG000248869; -.
DR   KO; K00850; -.
DR   OMA; RGLYNND; -.
DR   BioCyc; CCEL573061:GIXD-2983-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000002730; 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:UP000002730};
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:UP000002730};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|RuleBase:RU004092}.
FT   NP_BIND      79     80       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   NP_BIND     119    122       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   REGION      142    144       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      186    188       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      290    293       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    144    144       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   METAL       120    120       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      16     16       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     179    179       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     239    239       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   BINDING     284    284       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   SITE        121    121       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   366 AA;  39689 MW;  8637CA4940435B7C CRC64;
     MQEQKIKKIA LLTGGGDCPG LNAVIRAVTR TAILKYGYEV IGYIFGYRGL YNNDFIPLTL
     DKVSGIGHKG GTILYSSNKD NLFDYQVEEN GEIVKKDVSD VAIENLKKEG VDAIVVIGGD
     GTLTSARDFS RKGINVIGVP KTIDNDLPAT EVTFGFNTAV EVATEALDRL HTTAESHHRV
     MLLEVMGRNA GWIALHSGLA GSADVILIPE IPYDLHKVAE KIEMRQREGK KFTIIVVAEG
     AKPKDGDVVV AKVVDDSPDP IRLGGIANKL AADLEKIIKN QEIRATILGH IQRGGITSAY
     DRILSTRYGV AATELIHEGK FGNMVTLKED KISYEALEKV IGHTRVVEPD GELIQTARSI
     GVSFGD
//
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