ID A0A0T7BWN7_9CYAN Unreviewed; 783 AA.
AC A0A0T7BWN7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=IJ00_21305 {ECO:0000313|EMBL:AKG23476.1};
OS Calothrix sp. 336/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG23476.1, ECO:0000313|Proteomes:UP000065745};
RN [1] {ECO:0000313|EMBL:AKG23476.1, ECO:0000313|Proteomes:UP000065745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:AKG23476.1,
RC ECO:0000313|Proteomes:UP000065745};
RX PubMed=25614574;
RA Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA Battchikova N.;
RT "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT cyanobacterium isolated from a finnish lake.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP011382; AKG23476.1; -; Genomic_DNA.
DR RefSeq; WP_035156483.1; NZ_CP011382.1.
DR AlphaFoldDB; A0A0T7BWN7; -.
DR STRING; 1337936.IJ00_21305; -.
DR KEGG; calh:IJ00_21305; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000065745; Chromosome.
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; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
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; PS00742; PEP_ENZYMES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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:AKG23476.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000065745};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..328
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 365..436
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 483..771
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 783 AA; 87065 MW; B85D0EE6E19D1186 CRC64;
MKRLYWLDEI QSQNRADVGD QAFYLGKIKQ RGYPVLPGFV ISATVLREFL ETLNSTEALV
ADLPYSSLHL DVGNWRQLQQ VAGRLRQEII TAPLPEDFLE DIFTAARSWD NECLIFHPTL
IVPGKSAASV EGLMEAQVCC CQPEAIAMTL KQTWSQLFRA RSLLYWQQAG VDLQKIKLAV
LVQPLGKAIA SGIFNGNTAD WEIQSTWGLG MAITTGEVLP DVYYVKPLTT QVFEQQLGSK
ILEYSVKEKY HPLPELSAPQ FLLTVEQNCL QVELIDETKQ QEYALPEIHL HNLIALGNRF
AQQVSHHFTW EWTIRQDDSS GTLYITQVSA FTGINLNSHF LKGLGAATGI ITATAHVLYS
KPEEIPPGVI LIAPAIAPDW LPILQQAGGI VTEQGGLTSH GAILARELRI PAVVSISNVT
NLIQHGEQLL IDGEKGEVYR LSMMGEGEKP QKADIEDNLS LAPVAPQISD PHPSPDIFPS
SQLPIIATEL LVNLSQANLI AQVAKLPVDG IGLLRSELMA LTILEGKHPQ VWINEGKQAE
LLTRWCEHLS QFVRAFTPRP IFYRSLDWRS PELSSFHKNL PIASLSILGD RGTYSYMKNP
AVFNLELAAI AAVQKAGYEN IRLLLPFVRT VEEFSFCRQQ VEQVKLTASK HFQLWIMAEV
PSVLFLLDKY VKAGVQGISI GTNDLTQLLL GVDREQGELA QAFDEKHPVI MDAIAQLIRM
ARDNHIPCSI CGQAPALYPE IIQRLIELGI NSISVEPEAV IRTYQAIARA ESRILLANAR
NQF
//
