ID A0A0V7ZX04_9CYAN Unreviewed; 815 AA.
AC A0A0V7ZX04;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BC008_10035 {ECO:0000313|EMBL:KST62500.1}, BC008_34990
GN {ECO:0000313|EMBL:KST69120.1};
OS Mastigocoleus testarum BC008.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocoleus.
OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST69120.1, ECO:0000313|Proteomes:UP000053372};
RN [1] {ECO:0000313|EMBL:KST69120.1, ECO:0000313|Proteomes:UP000053372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC008 {ECO:0000313|EMBL:KST69120.1,
RC ECO:0000313|Proteomes:UP000053372};
RA Guida B.S., Garcia-Pichel F.;
RT "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT Mastigocoleus testarum strain BC008.";
RL Genome Announc. 0:0-0(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}.
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:KST69120.1}.
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DR EMBL; LMTZ01000154; KST62500.1; -; Genomic_DNA.
DR EMBL; LMTZ01000035; KST69120.1; -; Genomic_DNA.
DR RefSeq; WP_027846325.1; NZ_LMTZ01000154.1.
DR AlphaFoldDB; A0A0V7ZX04; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000053372; 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; 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.
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};
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:KST69120.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053372};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..318
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 371..442
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 515..802
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 815 AA; 91293 MW; 916E54AB70010248 CRC64;
MDKLYWLDRI QLQDRTKVGE KAFKLSTIKQ LGYPVVPGFV LEAEVMQEFL ESLNTSEALI
ADLPHSSLHL DADNWRQLQQ VAKNLRQEII NATVSPEWVK NITSAAQEWE SKYLVFRPSI
AIPHANNLRL ENISSVLETQ FCCNEFEAIS STLKRVWSQL FRAKSLFYWQ RIGIDLQQVN
FAVLVQPIES AIASGTLNSY HWGWEIEATY GLGIGITLGD ILPDFYSIEG ETLNIQKQQL
GNKILAYRIG DNQSTENSPA IATSSIVLNN NCLLPYILEE IKQQQYALSP QYLHQLNQIT
GQLIDEFGSN FSFNWTIFPE TPTGRIYLTK VNNPLSSINR LNKIRGLAAS TGKVKANTFI
INNSDPRPEL LPQGVILIAP NITPDWLPIL RNVAGIVAER GGLTSHAAIL ARELGIPAVV
NVPEVTSIFE QGEPILIDGD NGEIYRLSAD TEQTLDNGKN HQFSLNTKLA SNQNQPGNLS
TAVAVSMQHN SVPNDRNLLL PKDLPRSSSP NFEESIVATQ LLVNLSQSHL IEEVKNLAVD
GVGLIRSELM VLKILEGQHP RNWLRSGRRE QLLECWCQEI LQFVGNFNPR PVFYRSLDWR
SHELPSLQHH SQSSSQSILG ERGTLSYLQN PELFELELEA LANIQQAGYS NVNLILPFVR
TVEEFSFCRH KVEEAGLTRT QKFQLWIMAE VPSVLFLLPE YIKAGVQGIS IGTNDLTQLL
LGVDREQGQL AAIFDERHPV VMTAISELIQ MAKEGGIPCS ICGQAPALYP EVIDKLVEWG
ITSISVEPEA LKRTHSAIAR AEKRLILEAA RTRKN
//
