ID U4K5F1_9VIBR Unreviewed; 786 AA.
AC U4K5F1;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 Name=ppsA {ECO:0000313|EMBL:CCO60547.1};
GN ORFNames=VIBNI_B0757 {ECO:0000313|EMBL:CCO60547.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO60547.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO60547.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203527; CCO60547.1; -; Genomic_DNA.
DR RefSeq; WP_022561148.1; NZ_JXXT01000022.1.
DR AlphaFoldDB; U4K5F1; -.
DR STRING; 28173.VIBNI_B0757; -.
DR KEGG; vni:VIBNI_B0757; -.
DR PATRIC; fig|1260221.3.peg.4393; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000016895; Chromosome 2.
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:CCO60547.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 17..347
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 383..454
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 481..780
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 786 AA; 86627 MW; 202AE21F8D601292 CRC64;
MQQNVVWYDA LSMNDVDKVG GKNASLGEMV ANLANAGVKV PNGYATTSFA FNQFLESGGL
NERIYALLET LDVDDVQALK STGETIRNWV LEHPFTEELE ADIRRCYAEL GEGDEMLSVA
VRSSATAEDL PDASFAGQQE TFLNVRGIDA VIEAVKHVFA SLFNDRAISY RVHQGFDHKG
VALSAGIQRM VRSDKASSGV MFTLDTESGF DQVVFITSSW GLGEMVVQGS VNPDEFYVHK
PSLQAGHHSV VRRTLGSKLI KMVYAEGSEL GTQVETIDTS AEERSSFSLS DEEIQALAQQ
ALIIEKHYGR PMDIEWAKDG VTGELLIVQA RPETVRSRDD KNVMERFHLN QQSEALIEGR
AIGQRIGSGV VRVVESLDEM DQVQEGDVLV ADMTDPDWEP VMKKAAAIVT NRGGRTCHAA
IIARELGIPA VVGCGNATER LNNGAQVTVS CAQGETGYVY EGELDFEIRR SSVDDLPELP
LKVMMNVGNP DRAFDFATIP NEGVGLARLE FIINKMIGIH PKALLNYDDQ PSEIKAEIDQ
RIAGYENPVE FYIEKLTEGI STLAAAFWPK RVIVRMSDFK SNEYRNLVGG VRYEPTEENP
MLGFRGASRY ISEQFQDCFA LECEAMKRVR GKMGLKNVEI MIPFVRTVSE AASVIDLLAK
HDLRRGDQGL KVIMMCELPS NAVLAESFLK YFDGFSIGSN DMTQLTLGLD RDSGEIAHLF
DERNEAVKAM LSMAIQAANK AGKYVGICGQ GPSDHDDLAQ WLMEQGIDSV SLNPDTVLET
WLHLGK
//
