UniProt: Q4BWK1

Database: UniProt
Entry: Q4BWK1_CROWT

LinkDB:  Q4BWK1_CROWT 
Original site:  Q4BWK1_CROWT

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
All databases (23)   

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ID   Q4BWK1_CROWT            Unreviewed;       771 AA.
AC   Q4BWK1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE            EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996};
DE   AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470};
GN   ORFNames=CwatDRAFT_1078 {ECO:0000313|EMBL:EAM48281.1};
OS   Crocosphaera watsonii WH 8501.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM48281.1, ECO:0000313|Proteomes:UP000003922};
RN   [1] {ECO:0000313|EMBL:EAM48281.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48281.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   DOE Joint Genome Institute;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAM48281.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48281.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M.;
RT   "Annotation of the draft genome assembly of Crocosphaera watsonii WH
RT   8501.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAM48281.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM48281.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Crocosphaera watsonii WH
RT   8501.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001518};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAM48281.1}.
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DR   EMBL; AADV02000160; EAM48281.1; -; Genomic_DNA.
DR   RefSeq; WP_007307928.1; NZ_AADV02000160.1.
DR   AlphaFoldDB; Q4BWK1; -.
DR   KEGG; cwa:CwatDRAFT_1078; -.
DR   OrthoDB; 9765468at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000003922; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR006319; PEP_synth.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR   PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAM48281.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000313|EMBL:EAM48281.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003922};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAM48281.1}.
FT   DOMAIN          16..306
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          376..444
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          477..745
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   771 AA;  86185 MW;  39B97894AF3096CD CRC64;
     MIELYWLSEI DLRDRPVVGE KAWILSQLKQ SGYNVFPGFV ISASVFRDFL DNLNDVNSLL
     ADFPGSSLHL DVDNPRTLQL VAQQSRQSIL SVSFPAQWRD ILTEAARKLD SEALILRTSL
     GGTFPLNQDI SGLTPGKVCW NVADNLETAI KEMWAQLLNA KSLFYWQRLG IRIEELNLGI
     LIQPMVNSVA SGRIINQSKN YEIEGNWGLG NSLLQGDILP DYWKIEGESG QVLAQRLGNK
     SRAYSLRDKP ELTQLNSEEC LEVYCLSEQQ QSKYCLNSED ITKTFQLFKD LHDYAISWHC
     LEWILCNSAD NSSLELVIAQ LIPLPYNQFI KNTKSEIITE PSQPQLMGIG AAPGKTQGTV
     YLLNEDNSSH LVSSKHPIIV TQKIHPFQLS SIKQASGVVT EEGGITSHAA ILARELGIPA
     VVGVPGVTTW VQAGDSILID GDHGTIILNT SNHKEITLQP SPVSLEKTPS LDYPIGTQLM
     VNLTQPSSLG KIKGLPYDGL GLIRSELMLL DLCTPHSLKE WLGNFQRDEI VEKIKQRIIE
     FAQFFNPQPI FYRTFDDKFS AEQNRRGTAG YCLDSSLFRL ELQALSAVQK QGYENINVIL
     PFVRTVNEFR FCLDLIDEFK LSSSSSFQVW IMAEVPSIIF QLADYVKAGV QGIAIGTNDL
     IPLLLGIERN NLSWNNIPAV YESSIYGALK QLIEEAYKLG IPSSVCGQVI VNYSPIIEKL
     VNWGITTISV EPEAIEKTYQ AIARTEQRLL LALARETKKN LESRINNNHI T
//

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