ID A0A0K2M0L6_9NOST Unreviewed; 955 AA.
AC A0A0K2M0L6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:ALB41593.1};
GN ORFNames=AA650_14990 {ECO:0000313|EMBL:ALB41593.1};
OS Anabaena sp. WA102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB41593.1, ECO:0000313|Proteomes:UP000056652};
RN [1] {ECO:0000313|EMBL:ALB41593.1, ECO:0000313|Proteomes:UP000056652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA102 {ECO:0000313|EMBL:ALB41593.1,
RC ECO:0000313|Proteomes:UP000056652};
RA Brown N.M.;
RT "The finished genome of an anatoxin-a-producing Anabaena isolate reveals
RT extensive genome rearrangement.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011456; ALB41593.1; -; Genomic_DNA.
DR RefSeq; WP_053539605.1; NZ_CP011456.1.
DR AlphaFoldDB; A0A0K2M0L6; -.
DR STRING; 1647413.AA650_14990; -.
DR KEGG; awa:AA650_14990; -.
DR PATRIC; fig|1647413.5.peg.3544; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000056652; 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; 1.
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:ALB41593.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyruvate {ECO:0000313|EMBL:ALB41593.1};
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 83..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..444
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 879..950
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 955 AA; 104990 MW; 2A2B43EF1E70DD81 CRC64;
MINLFGIVII LIVCPLLGAI PLISWITYAL SGKQLAKVGT GNISVAAAFY HGGKLAGSIC
VVSEALKGVG VVTIAQYCFP SQPVWELIAL IALVIGRYVA TKGAGITNVS WGLLAHDPMV
AAFVSLLAAM GFLITRSKET IKLGVLVIFP LFVGIIHSQD ILRIIAAATL SGLIYWIYSQ
IPDDMNLPVE EAALESQPMM EYLNNQERII TLDDDLDGEV VGAKAATLSQ IKRWGYAVPK
GWVLPAGEDP TVLIDFLQPS PLSPLVVRSS AIGEDSQQAS AAGQYETILN VISKVELRQA
IAQVKASYDH PSAVEYRHRS SSEDRAMGVL IQQQVQSVFS GVAFSRDPIS QQGEAVVIEA
VSGSPTQIVS GKVTPEQYRV VVADNEKLSC LQFEGHGKVP EALIKQVAYL ARRLEKRYLG
IPQDIEWSYD GQNLWVLQTR PITTLLPLWT RKIAAEVIPG VIHPLTWSIN SPLTCGVWGE
IFSIVLGDRS NRLDFTTTAT LHYSRAYFNA SLLGEIFLKM GLPPESLEFL TRGASMSKPA
LDSTLANLPG LTKLLKREID LDKDFKLDYR QVFIPGLTQL SNVVIEELSL DQLLGRIDLI
LDLLHRGTYY SILAPLSAAI RQAVLGAKVE EIDNSVTPEV ASLRAMRLLA ADARQILIAG
NYEFKPEQVF AQLAETAAGS RILAEFNELI EDYGYLSEVG TDISVPTWRE NPQIVRQLFI
QLLQAPEAPN LDDSRSEQTN LVQRRVDLKG RVTEVYSRLL AELRWTFLAL EQMWLQSGVL
TQQGDIFFLK LEEIRRLGIN PDVAFRNHIW ELIANRRSQF IQDSQIPQIP PVVYGYNPPH
PIKPVIDSSD NILLGIPASQ GQIQGRVKVL RTLQEAHNID KNTILVVPYT DSGWAPILVQ
AGGLIAEAGG KLSHGAIIAR EYGIPAVMDV RGATYLLQDG QQVQIDGYKG TVEIL
//
