ID K9Z7G5_CYAAP Unreviewed; 964 AA.
AC K9Z7G5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:AFZ54520.1};
GN OrderedLocusNames=Cyan10605_2439 {ECO:0000313|EMBL:AFZ54520.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ54520.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
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; CP003947; AFZ54520.1; -; Genomic_DNA.
DR AlphaFoldDB; K9Z7G5; -.
DR STRING; 755178.Cyan10605_2439; -.
DR KEGG; can:Cyan10605_2439; -.
DR PATRIC; fig|755178.3.peg.2583; -.
DR eggNOG; COG0344; Bacteria.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_3; -.
DR Proteomes; UP000010480; 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; 2.
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:AFZ54520.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyruvate {ECO:0000313|EMBL:AFZ54520.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010480};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..387
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 391..440
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 881..952
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 964 AA; 108274 MW; 115223C608E35E17 CRC64;
MTQIGGILSI LIIPPIIGAI PLIDWFTYAV SGKELTKLGT GNISVSAAFY HGGKLAGILA
VLSEAGKGVG VVLLSRIFFP SGSFWEIIAL IMLILGRYYL GKGAGATNLT WGIVTHNPVA
ALLIFILGGV SFTIWREKRA GRISVLVLMV VVLSAQNINH PEYILLTIIL ASLMIWIYRQ
MADDLELNPS EVNGESAKMF RFFRGDSGII SLNEALNPQK VGAKASNLSR LKKWGYNVPD
GWVLKIGDDI HKLQEFINPS SSNPYVVRSS ALDEDTNWAS AAGIYDSFVD LTDFDHLSQA
VIDCFSSYNS AIALDYRQRQ KQSEKGIAVI IQKQINGIYS GVIFSRDPVN QLEDTVCIEA
VSGMGLKLVS GEVTPQQYRV FFPEEKVEGE GDISQEVLLN LGKIAREIEH LCQGIPQDIE
WTYDGEKIWL LQTRPITTLK PVWTRKIAAE VIPGVIRPLT WSINQPLTCG VWGEIFTIVL
GKKSRKLDFS QTATLHYDHA YFNATLLGEI FLLMGLPPES LEFLTRGSKF SKPPLTATIV
NLGGLWRLLR KEWRLITDFA HDNDRYFRPI LDELKDIPCE TLSTIELLDR IDHILEVLKK
ATYYSILAPL SYSLRQTIFQ VNPNDLDYDK IPEITSIKSL QKIAIETQNL LSEAELNQLD
CNNYPAFFSY LSESTEGESI LNRLEKWLEE YGYLSETATD IAVSRWSEDQ SHMRLMFSKF
VGEKEIILKV NKDKNKSWKT SMVQPRLDLK GQVAEIYSKL LAYLRYSFVE IENKLIKEKK
VLEQGDIFFL KLTEIKDLIK DETINIDKIY NLIKARKCTW EENKKIKKIP YLIYGETPQI
DLTTQNDIST TKKSLQGIPA SMGIKEGKIK IIKSLTEAKN IDRETIIVVP YTDAGWTTIL
TQAGAIISEV GGKLSHGAII AREYHIPAVM DIPHATEIFH DGQLVKVNGN NGIVTILSQI
TIEH
//
