ID A0A225N366_9BURK Unreviewed; 797 AA.
AC A0A225N366;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623, ECO:0000256|PIRNR:PIRNR000854};
DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996, ECO:0000256|PIRNR:PIRNR000854};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470, ECO:0000256|PIRNR:PIRNR000854};
GN ORFNames=CEY11_01675 {ECO:0000313|EMBL:OWT65479.1};
OS Candidimonas nitroreducens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Candidimonas.
OX NCBI_TaxID=683354 {ECO:0000313|EMBL:OWT65479.1, ECO:0000313|Proteomes:UP000214603};
RN [1] {ECO:0000313|Proteomes:UP000214603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-089 {ECO:0000313|Proteomes:UP000214603};
RA Fan M., Lin Y.;
RT "Herbaspirillum phytohormonus sp. nov., isolated from the root nodule of
RT Robinia pseudoacacia in lead-zinc mine.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988,
CC ECO:0000256|PIRNR:PIRNR000854}.
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 ECO:0000256|PIRNR:PIRNR000854};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000854};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000854}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000854}.
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:OWT65479.1}.
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DR EMBL; NJIH01000002; OWT65479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225N366; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000214603; 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 NCBIfam; TIGR01418; PEP_synth; 1.
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 PIRSF; PIRSF000854; PEP_synthase; 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, ECO:0000256|PIRNR:PIRNR000854};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000854};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000854};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000854};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000854}; Pyruvate {ECO:0000313|EMBL:OWT65479.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000214603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 16..348
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 382..453
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 479..788
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 797 AA; 87605 MW; 584751B3408607FE CRC64;
MSYVVSFEQL RMSDVDSVGG KNASLGEMIS QLADAGVRVP GGFATTAQAF RDFLKSTGLD
VRINQRLDAL DADDVRALAE AGAQIRQWVI DTPFPAQFEQ AIREAFAQLD ADGKGTFAVR
SSATAEDLPD ASFAGQQETY LNVAGIDDVL EKIRHVFASL YNDRAISYRV HKGYQHADVA
LSAGVQRMVR SDRGSAGVMF TLDTESGFDG VVFITSSYGL GETVVQGAVN PDEFYVFKPT
LASGHYPIIG RRIGSKLIKM EFDPERTGGV AVRTVDVPVS ERNRYSLTDD EVIELARYAV
IIEQHYKRPM DIEWGRDGID GKIYILQARP ETVRSQQSQH DVQERYRLKA TGEVLVTGRA
IGQKIGSGTV RIVADISEMD QVRAGDVLVT DMTDPNWEPV MKLASAIVTN RGGRTCHAAI
IARELGIPAV VGCAHATSVL DNGHEVTVSC AEGDEGRIYD GLIETEIEEV RWGQMPEIGV
KVMMNVGNPQ LAFDFSQIPN QGVGLARLEF IINNNINVHP KAVLDYPNVD SDLKKAVESA
ARGYASPRAF FVEKLAEGVA TIAAAFHPKP VIVRLSDFKS NEYRKLVGGS RYEPEEENPM
LGFRGASRYI SAEFEECFRM ECEALKKVRD DMGLTNVEIM VPFVRTLQQA DKVVKLLARH
GLARGENGLR LIMMCEVPSN ALLADKFLQY FDGFSIGSND MTQLTLGLDR DSGMELLAAD
FDERDEAVKF MLNRAIKACL AAGKYVGICG QGPSDHLDLA LWLRDEGILS MSLNPDTVVD
TWQRLAQEEK SLQQDAA
//
