ID A0A1L9QWY3_9CYAN Unreviewed; 962 AA.
AC A0A1L9QWY3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:OJJ27198.1};
GN ORFNames=BI308_01535 {ECO:0000313|EMBL:OJJ27198.1};
OS Roseofilum reptotaenium AO1-A.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Roseofilum.
OX NCBI_TaxID=1925591 {ECO:0000313|EMBL:OJJ27198.1, ECO:0000313|Proteomes:UP000183940};
RN [1] {ECO:0000313|EMBL:OJJ27198.1, ECO:0000313|Proteomes:UP000183940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-A {ECO:0000313|EMBL:OJJ27198.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJJ27198.1}.
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DR EMBL; MLAW01000002; OJJ27198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9QWY3; -.
DR STRING; 1925591.BI308_01535; -.
DR Proteomes; UP000183940; Unassembled WGS sequence.
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; 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:OJJ27198.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyruvate {ECO:0000313|EMBL:OJJ27198.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183940};
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 88..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..448
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 884..954
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 962 AA; 106198 MW; B09274EBFF27E8BF CRC64;
MSIELLKGLT ILIFCPLLGG TPLIQWLTLA LTGKDLARLG TGNISVSAAF YHGGKLAGIG
AVLSEAGKGI GAVLLARSLF PQTPVWEIIA LIALVLGRYF ISQAAGTTNA TWGLVVHNWQ
ISLLVGLIAL IGLTVVRERK SRQYGILILF PLLQILMHPS DKGLAIATIS LNTSLALIYQ
HIPDDLELPS NSSTRNPNMP SLFPGNKGIL SLDRPLKAQE VGAKAANLAY LKKLGYPVPP
GWILLPGDDP QPVISLLNPS SQNPLIVRSS AFGEDTLHSS GAGQYTSIPQ ITNAQGLHQA
ILTCMRSADN PQAIAYRQSR QLPDTQVAVL IQQQIAGVFS GVAFSRDPIA RSGEDVIIEA
LPGDPSRVVS GQVTPESYRV LVIETDGEPT TQILEGDGDI PPALIHQVAQ ITRQIEGNYH
GIPQDIEWTH DGQQLWILQT RPITTLSPIW TRKIAAEVIP GFIHPLTWSI NQPLTCGVWR
DIFALVLGKK IANLDLNQLA TLHHSVAYFN ASLLGEIFRQ MGLPPESLEF LTRGAKFTRP
PLSSTVKQIP GLWRLLQREW SLEEDFERDN RKWFSPTLEQ LKNQAPQTPS ECLDRVDLIL
ETLKRATYYS ILAPLSFALR QAVFQVSEED LDYQEMPEVA ALEALQELAT CAHHLLPHLE
TETPETLFGC LSELPDGQSI IDQLCQFMED YGYLSEVATD ISVPRWRDNP RMVRDMFLQQ
LHQMKGDRPK TLPKRLKIQM VQVRLNLKGQ VTQVYSQLLA QLRWSFLALE NFWIESGILQ
TQEDIFFLTL PEVQAVLSDS TDTFLSTDRI PEIIATRRAT FAQDKLVKSI PYVAYGNQPI
KRITPSAQSR LKEGQTLSGI GASPGQAEGR VKIMRQLQNV EAVDTDTILV VPYTDSGWSL
VLAKAGGLIS EVGGRLSHGA IVAREYGIPA VMDIPNIMER LHDGQWVRID GETGMVEVMN
NE
//
