ID A0A1D7XXZ7_9FLAO Unreviewed; 1455 AA.
AC A0A1D7XXZ7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=FORMB_11550 {ECO:0000313|EMBL:AOR28201.1};
OS Formosa sp. Hel1_33_131.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1336794 {ECO:0000313|EMBL:AOR28201.1, ECO:0000313|Proteomes:UP000094750};
RN [1] {ECO:0000313|EMBL:AOR28201.1, ECO:0000313|Proteomes:UP000094750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_33_131 {ECO:0000313|EMBL:AOR28201.1,
RC ECO:0000313|Proteomes:UP000094750};
RA Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S., Kappelmann L.,
RA Chafee M.;
RT "Glycan utilization in Formosa spp.";
RL Submitted (SEP-2016) 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}.
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DR EMBL; CP017260; AOR28201.1; -; Genomic_DNA.
DR RefSeq; WP_069676507.1; NZ_CP017260.1.
DR STRING; 1336794.FORMB_11550; -.
DR KEGG; for:FORMB_11550; -.
DR PATRIC; fig|1336794.4.peg.1139; -.
DR OrthoDB; 1373043at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000094750; 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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.1260; Lamin Tail domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF07705; CARDB; 1.
DR Pfam; PF00932; LTD; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR PROSITE; PS51841; LTD; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000094750};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1455
FT /note="Phosphoenolpyruvate synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009102370"
FT DOMAIN 1214..1380
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
SQ SEQUENCE 1455 AA; 160325 MW; 88229170FF58ECBF CRC64;
MTKNFFLSLL CLISVYNFCF AQVPIDNYSV NGLGQVQLSI QAQAGKYYVL HAQHSSTFNW
ATSMTIGVSG TMIISESLSA YPIENYSITE HNVSAPDDYD GDGIDDITEF NNMPTDAPFN
FAPPIELIDG STSIPDVETF MELATINNVG WAPFLDDQMY VKFGILDRDT TEPQVYFINS
NTYTIHASFW GGIGASVTGD DSSGEIVFNP NDILPSGVIG TYSVNFSFGN AYDFEATQRT
YELLAASMPF LQNNMNHFIG QSDENDHINN HADDFVGSRI DVVLESDVFA EINYIPFHEA
EGYGFFKHMT DLNETPGSRD IVLYDALPNS LPRVGGIITS VIQTPLSHVN LRAIQDNVPN
AYIANPLAND AIANLLGGYI YYKVENEQYE IREATLTEVN DWYEELRPTE PQTPIRDLSI
TEIMPLDDIA FEMSTAFGAK CANVATMRSF ELPAGTIPDG FGIPFYYYDE FMQFNNFYQE
AQIMIDNPSF QTDLNFRIDR LKDFRRAIKD APMPQWMLDN LQVMHDDFPE GTAVRCRSST
NNEDLPGFSG AGLYTSKTQY LDEGHISKSI KQVYASMWNF RAYEERDFYR VNHFIAAMGL
LCHPNFQEEK SNGVGISIDP IYETEDTFYL NTQVGESLIT NPDPNSVPEE LLLYEDPTQG
GGYLVLRLSN LVNPGELVMD QVYIDQMRDF LTVIHDGFAV LYDVVGADDF GIDIEYKVTA
QDQLVIKQAR PWVSFWANIN GDNDLGITAI TEPQSSSNLG SNELVTITIA NQGLNPMSNF
DIELVVDGQS METITISQTI EPFTEADFQF TVPQDFSAIG EYSVTAIVSH PDDEYENNDT
LNVVLSKVHV LDAALSIGEV SVLCDDVVEV SASIANQGYT TITDVQIEVV VNGSVVEMLN
AAVDIPFLEQ ATVTIMIDNN LQENNTITLN VLNVNNQIDG DGTNNSASTT TTLDSNYDTI
TLIINADNYP QETSWKLVDE ANQIINTGSL SNGTEFYSED ICVNYSSCFT LYFYDSYGDG
ICCGFGEGNF QIIDASGNTI LTNDGEFDNF VKEVFCLDES ECDITVDINI SHATSSSAND
GVITINTNSG LSSYQYSIDG GETFTDSNTF DNLAPADYNV VVLGAAGLCS FEETVSVESC
NFISVDIEAT AVSSVVSTNG SIVITPTSGV GPYQYSIDGG QTFSQNNVFS NLAVGDYNVV
VKDIADICSY EVDVPIEVEG LVINEINYKS SVTFNPGDWI ELYNPKAGTI DISNWQIKDD
NDTHVFVIPE GTQIAGNGFL VLVKDAAAFS SVFPNIPYIG ELDFGFGGSD AVRVYNSDSK
LMDDVSYDSI APWPTCADET GNTLELITPD LDNELPENWS CINDNGSPNA VNSGGLSIND
LDPHSITVYP NPVNNTLYIA GNSERYDIEV YSLLGQRVMT ASNSSEIDVS SFNEGIYLIK
ISTENTTTVK RIVKF
//
