ID A0A235IJ31_9NOSO Unreviewed; 782 AA.
AC A0A235IJ31;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CDG76_04215 {ECO:0000313|EMBL:OYD98029.1};
OS Nostoc sp. 'Peltigera membranacea cyanobiont' 210A.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2014529 {ECO:0000313|EMBL:OYD98029.1, ECO:0000313|Proteomes:UP000215440};
RN [1] {ECO:0000313|EMBL:OYD98029.1, ECO:0000313|Proteomes:UP000215440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=210A {ECO:0000313|EMBL:OYD98029.1,
RC ECO:0000313|Proteomes:UP000215440};
RA Gagunashvili A.N., Andresson O.S.;
RT "Distinctive characters of Nostoc genomes in cyanolichens.";
RL Submitted (JUL-2017) 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:OYD98029.1}.
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DR EMBL; NOLJ01000001; OYD98029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235IJ31; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000215440; 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};
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:OYD98029.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..338
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 370..441
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 482..769
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT REGION 450..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 86431 MW; 432ADDD2F8277FC7 CRC64;
MNKLYWLDQI KLQDRAKVGD KAFYLSKIIQ RGYPVMPGFV VSAEILRQFL ENLNSSESLV
ADLPHSSLHL DVTNWRQLQQ VASRLRQEIL SATVTQEWVS PIFQAAKEWQ TSCLILRPSL
TVSTATPGIN NNISGLLESV FCQCEPEAIA LALKRTWSQI FRARSLLYWQ HLGINLQQIN
LAVLVQPVGN AIASGSLTTN SSGWEIEATW GLGIAIAQGE VQPDVYYIQP ETGVVLEQQL
GNKMLAYGVD DAAPKVFSQP LPNSALTPDH TCLITYLLPE AQQKQYSLQE EYLQQIIALG
TQLVSELGKT FTIKWTIAEQ PTSGKLYITQ VSPSQSISHT HFIRGLGAAG GRVVATALVI
INSQQKPEQL PKGVILVVPT ITPDWLPLLQ QVAGIITEQG GLTSHAAILA RELGITAVVN
ATSATTLIQT GERLLLDGDR GEVYRIKGDS KEEMERGREE NLLSSHYPNP KASHPAVTSH
LPMIATQLLV NLSQSTLIEQ VQNLPVDGVG LLRSELMVLN ILNGQHPNSW ILSGRQAELL
ELWSEQIMQF ARAFAPRPVF YRSLDWRSQD LPSLRDSLES SPQSMLGERG TFSCLRNPAV
FELELKALAS VQEAGYTNVN LLLPFVRTVE EFVFCRRKVE QAFLTEVAQF QLWMMAEVPS
VLFLLPEYVK AGVAGISIGT NDLTQLLLGV DREQGQLAKV FNERHPAVMG AIAQLIQMAR
SAGIPCSICG QAPALYPEII DKLVEWGITS ISVEPEAVER TYQAIARAEQ RIILAAARRK
LH
//
