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Database: UniProt
Entry: A0A0R1LRN4_9LACO
LinkDB: A0A0R1LRN4_9LACO
Original site: A0A0R1LRN4_9LACO 
ID   A0A0R1LRN4_9LACO        Unreviewed;       871 AA.
AC   A0A0R1LRN4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138};
DE            EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
DE   AltName: Full=Pyruvate, orthophosphate dikinase {ECO:0000256|ARBA:ARBA00032883};
GN   ORFNames=FD04_GL000216 {ECO:0000313|EMBL:KRK98485.1};
OS   Secundilactobacillus odoratitofui DSM 19909 = JCM 15043.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1423776 {ECO:0000313|EMBL:KRK98485.1, ECO:0000313|Proteomes:UP000051160};
RN   [1] {ECO:0000313|EMBL:KRK98485.1, ECO:0000313|Proteomes:UP000051160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19909 {ECO:0000313|EMBL:KRK98485.1,
RC   ECO:0000313|Proteomes:UP000051160};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR000853-3};
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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:KRK98485.1}.
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DR   EMBL; AZEE01000027; KRK98485.1; -; Genomic_DNA.
DR   RefSeq; WP_056946818.1; NZ_AZEE01000027.1.
DR   AlphaFoldDB; A0A0R1LRN4; -.
DR   STRING; 1423776.FD04_GL000216; -.
DR   PATRIC; fig|1423776.4.peg.215; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000051160; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.80.30; -; 1.
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   Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
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; IPR010121; Pyruvate_phosphate_dikinase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR   PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR   PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF01326; PPDK_N; 2.
DR   PIRSF; PIRSF000853; PPDK; 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};
KW   Kinase {ECO:0000313|EMBL:KRK98485.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000853-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000313|EMBL:KRK98485.1};
KW   Transferase {ECO:0000313|EMBL:KRK98485.1}.
FT   DOMAIN          57..299
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          302..351
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          420..501
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          518..866
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        453
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT   ACT_SITE        828
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT   BINDING         559
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         615
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         742
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         742
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         763
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         764
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         765
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         766
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         766
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ   SEQUENCE   871 AA;  95547 MW;  91EB8A796E707C55 CRC64;
     MTKQIYAFSE GNMSMRDLLG GKGANLAEMT NLGLPVPHGF TLTTEACHRY QETGSLSSEL
     LTELDEALAT LSQTTGKQFN GDTQPLLVSV RSGAAISMPG MMDTILNIGL NDQTVVALAT
     LTNNERFAYD SYRRLLAMFG NVVYNIEEET FDHVLTDLKQ QKGYDSDLEL TADDLKQIVA
     DFKAIYQAAG KGEFPQSPKD QLLAAVNAVF ESWNNHRAQV YRQQNHISES LGTAVNVQEM
     VFGNAGEQSG TGVAFTRNPA SGEKKVFGEY LLNAQGEDVV AGIRTPETIE VLKDAMPVIY
     DQLMGIAEKL ENHYQDMQDL EFTIENGKLF LLQARDGKRT PYAAVKIAVD QVGEGLITKE
     QALKRVSPES VSAMLHPEFD ETDLGQHTKL TTGLPASPGA ATGRAYFTAE DAKRASDGGE
     QVILIRQDTS PEDIEGMIVS QAIVTSRGGM TSHAAVVARG MGATGVVGAH EITVDYAGKV
     AKVGDQVIHE GDWVSVDGTT GNLYLGQINT TPAGVKGELS TLLDWAKDVA KMGVYTNADT
     PQDFQKALDF DADGIGLTRT EHMFFKPERL LQMRRLILAT DAKGRRDPLS QLLQMQQEDF
     YQLYKLAGDK EVTIRLLDPP LHEFLPHDEA EIQIVANQIQ ETPERLRERI TSLKELNPML
     GHRGDRLAVT FPDIYQMQVK AIMSAVIRLN DEGLEVHPHI MIPLTDSRDE MSWVRDLVTD
     QIQQMVNNSG IRVDYTVGTM MEMPRACVTA DQIAEVSDFF SFGTNDLTQL TFGYSRDDVG
     SFMPEYIKQG ILPADPFQTI DTQGVGALME IAITKGRQTN PELPIGVCGE VGGDPASIEF
     FNQIGITYVS CSPYRVPVAR LAAAQATLTQ N
//
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