ID A0A0M5KTM3_9MICC Unreviewed; 797 AA.
AC A0A0M5KTM3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AL755_09945 {ECO:0000313|EMBL:ALE05716.1};
OS Arthrobacter sp. ERGS1:01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE05716.1, ECO:0000313|Proteomes:UP000060433};
RN [1] {ECO:0000313|EMBL:ALE05716.1, ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE05716.1,
RC ECO:0000313|Proteomes:UP000060433};
RX PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT bacterium with prospective cold active industrial enzymes, isolated from
RT East Rathong glacier in India.";
RL J. Biotechnol. 214:139-140(2015).
RN [2] {ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL Submitted (AUG-2015) 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}.
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DR EMBL; CP012479; ALE05716.1; -; Genomic_DNA.
DR RefSeq; WP_054010870.1; NZ_CP012479.1.
DR AlphaFoldDB; A0A0M5KTM3; -.
DR STRING; 1704044.AL755_09945; -.
DR KEGG; are:AL755_09945; -.
DR PATRIC; fig|1704044.3.peg.1246; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000060433; 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; 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:ALE05716.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000060433};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 17..345
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 386..457
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 481..788
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 797 AA; 86029 MW; 42155E4DF96146B9 CRC64;
MTTDILWFSE LGLKDLDRVG GKNASLGEMV GNLKNAGVRV PDGFATTADA YRRFLRETGV
EAKIAGILAD LDIDDVRALA EAGSAIRHAI VQTPFPADLE AQLRTAYEEL VTKHGGAGDL
SWAVRSSATA EDLPDASFAG QQETFLNVRG IENILAAVKD VFASLYNDRA IAYRVHHRFE
HLDVALSAGI QRMVRSDVGA SGVMFTMDTE SGFQGAVFVT SSYGLGEAVV QGAVNPDEFY
VYKDGLKAGR PAILKRGLGD KALTMVYTAS EEVGHTIELI PTVPELRSRF SITDDDVEQL
ARHALAIEEH YGRPMDIEWG KDGVDGELYI LQARPETVES RKSAGTLSRY RLEGSGPVLA
EGRAIGQRIG SGPVRILASI DQMAEFTTGD VLVADMTDPD WEPIMKRASA IVTNRGGRTC
HAAIIARELG IPAVVGTGDA SVALAEGAQV TVSCAEGEAG FIYAGLLDFR VEETELDSLP
EAPVKVMMNV GTPEQAFTFA QLPNHGVGLA RLEFIINRQI GIHPKALLNL ADQPDDVADI
INERIAAYDG PVDYYVKRLA EGVATIAAAF APETVIVRMS DFKSNEYANL IGGPAYEPHE
ENPMIGFRGA SRYLEPSFRD CFDLECEALA FVRNDMGLSN VKLMIPFVRT LEEGRGVIEL
LAENGLCRGE NGLEVVMMCE VPSNALLAEE FLEIFDGFSI GSNDLTQLTL GLDRDSAIVA
ASFDERNAAV KKLLSMAIRA CKAKGRYVGI CGQGPSDHLD LAEWLVGEGI DSISLNPDTV
VDTWLRLATM EPGHANP
//
