ID K9RWV8_SYNP3 Unreviewed; 953 AA.
AC K9RWV8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Phosphoenolpyruvate synthase/pyruvate phosphate dikinase {ECO:0000313|EMBL:AFY62026.1};
GN OrderedLocusNames=Syn6312_2968 {ECO:0000313|EMBL:AFY62026.1};
OS Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY62026.1, ECO:0000313|Proteomes:UP000010379};
RN [1] {ECO:0000313|Proteomes:UP000010379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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DR EMBL; CP003558; AFY62026.1; -; Genomic_DNA.
DR AlphaFoldDB; K9RWV8; -.
DR STRING; 195253.Syn6312_2968; -.
DR KEGG; syne:Syn6312_2968; -.
DR PATRIC; fig|195253.3.peg.3002; -.
DR eggNOG; COG0344; Bacteria.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_3; -.
DR Proteomes; UP000010379; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 2.
DR SMART; SM01207; G3P_acyltransf; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:AFY62026.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyruvate {ECO:0000313|EMBL:AFY62026.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010379};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..379
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 398..441
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 875..946
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 953 AA; 104026 MW; 3B5867B5F71FA5BC CRC64;
MITQIGLAIV LGLGCSVLGG LPIINGLGLL WLKRPLSQLG TGNAGVSAAF YHGGTVLGIL
AVCSEAAKGI LAVLWMQNWF PDLAVGPWLA LLCLVAGRYC WGNGAGTTNV VWGVLWFAPG
VAWLTVLVSG VSFTIFRQRQ QGRLVALIIF PVMVALIRRS IPETLAAGVL ALTLGWIYEE
LPDDLALNRH QARPESQVMF QFFQGERALL SLDHPLSPEK VGHKAATLSQ LKRWGYAVPM
GWVLPAGDDP EPLITSLNFD VAHPLVARSS APGEDSLASA MAGQYASFLD ITNPEQLTQA
LIGVQQSYNR ANNPSESDHS NHAGMAVLVQ IQIQGVFSGV AFSRDPLWGG LDCVAVETLP
GPASRVVSGQ FTPESYRVLF DAQGPIPDSL KITGDVPAAV ILEVARLCRE LETRYHGIPQ
DLEWTYDGQT IWVLQARPIT TLLPIWTRKI AAEVIPGVIH PLTWSINRPL TCGVWGEIFS
LVLGQAAQGL DFQATADLHF GRAYFNATLL GTIFRRMGLP PESLEFLTRG AKMSRPPLST
TLKALPGLGK LAQREWQLPR DWQRDDQKHL HPLLQELQEH PITAAADPLW LLNRIEKILT
GLEIATYYNI MAPLSAALRQ ALGRVHPETL DTSTSPETAS LKALTTIAQK VQEILKTDVA
TAPEPLKQAL EKMPEGKTVL GDLEKFLQTF GYISPTATDI SVPTWQETPD LVWQLLGSLV
GQSTSAHRPK FNPKAQAWVQ ARINLKGDVA TVYGQLLANL RWTVLGLENQ WLKNGQLLTK
GDIFFLQFNE LTTAIQAPQT MDWPNYQELI ENRRREFNAL QNLEPIPYVV YGQNPQLPIS
VTQQQTSTWQ GIGASPGIAQ GRVQIIHNPS QALRVPPNTI VVVPYTDAGW LPVLTGAVGI
ITEVGGRLSH GAIVARELGI PAIMGLEQAT QHLKTGQQIQ MNGQTGKITL LET
//
