ID F6GIB2_LACS5 Unreviewed; 967 AA.
AC F6GIB2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 OrderedLocusNames=Lacal_2456 {ECO:0000313|EMBL:AEH02298.1};
OS Lacinutrix sp. (strain 5H-3-7-4).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lacinutrix.
OX NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH02298.1, ECO:0000313|Proteomes:UP000008297};
RN [1] {ECO:0000313|EMBL:AEH02298.1, ECO:0000313|Proteomes:UP000008297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH02298.1,
RC ECO:0000313|Proteomes:UP000008297};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
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; CP002825; AEH02298.1; -; Genomic_DNA.
DR RefSeq; WP_013871077.1; NC_015638.1.
DR AlphaFoldDB; F6GIB2; -.
DR STRING; 983544.Lacal_2456; -.
DR KEGG; lan:Lacal_2456; -.
DR eggNOG; COG0574; Bacteria.
DR HOGENOM; CLU_012700_0_0_10; -.
DR OrthoDB; 1108665at2; -.
DR Proteomes; UP000008297; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:InterPro.
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 InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEH02298.1};
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:AEH02298.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008297};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 621..946
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 967 AA; 109284 MW; 44FFBFB02F2803CC CRC64;
MLKNTFFTFI LFYAFISYSN AQQRTTKQIK NLIETYKNDP RGPYHRIKWF CKDGTEREPR
DPCPDDIGGG IQHAAFKTTA LDLRKTNNLY FGEIIAALEP KDFLDHNNNY SRLKQYQLGK
YLASVDNGWV LQKAQFYRGA IQSEDEEAWG KDFFEWLLKD EQIITSKYYL LRQALKDIPH
NGDDNIAQLM RSQSKTLSED LKSFMDIRIK IHGQPEVTDI KLVKDYIANN TIPNDLKKGF
DELVETMYKF YSPIDFSKLE KELNKLPVSN PTTLKIKAFI TSNKNQKTSA SFVSEIASIL
TEIRENILSY KNSKHRLQLL DLSNQLEHTL LTETQNWQIN TVGESLDKIN ALTCAAMGTG
LIEIWEYNAI ENTLNNKIAQ NNLTLYELNQ LLTTSRSVVE WSASTVKANY QDIVGKYTAF
EPLSYGFIDD RIRSSIALNL GETVSLFGAF IAKTSHINNS VMAIENQSAI RGLNPGYAYG
ELVVVDGNPD NIEVNTNKIY IFEKPPHDLK PVAGIMTVSE GNLVSHVQLL ARNLGIPNAA
LSYNNLKELK KHNGETVFYA VSNKGNVILK TEDDMSSIEK KLFNKKERNK NVIAVPVDQI
RLDVSKVINM RDVDASDSGK LCGPKAANLG ALKKMFPKQV VEGIIIPFGI FRTHMDQQMP
NQNKTYWQYL NSTFNTAKAM REANKSDEVV EKFQLDALEV LHKAIINMPL EAAFLNDMKS
SFASAFGDAI GNVPVFLRSD TNMEDLKEFT GAGLNLTLFN IKAEDEIIKG IKRVWASAYT
ERSFKWRQKY LSNPENVFPS ILIIPSVDVD YSGVMITKGI NSGNDEDLTV AFSRGAGGAV
DGQSAETRLI TSKANVLLAP ARQSDYIRLP DYGGTKQYTT SFETPILNQQ NIKDIRTLAS
EIRKTMAKHN DDAKQAYDVE FGFKNNKLWL FQIRPFVENK QAKSSEYLSS IAPNTDSKQT
INLSEKL
//
