ID M1WYF9_9NOST Unreviewed; 942 AA.
AC M1WYF9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Similar to phosphoenolpyruvate synthase {ECO:0000313|EMBL:CCH66847.1};
GN ORFNames=RINTHH_6920 {ECO:0000313|EMBL:CCH66847.1};
OS Richelia intracellularis HH01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Richelia.
OX NCBI_TaxID=1165094 {ECO:0000313|EMBL:CCH66847.1, ECO:0000313|Proteomes:UP000053051};
RN [1] {ECO:0000313|EMBL:CCH66847.1, ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|EMBL:CCH66847.1,
RC ECO:0000313|Proteomes:UP000053051};
RA Hilton J.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|Proteomes:UP000053051};
RA Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P.,
RA Villareal T.A.;
RT "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen
RT metabolism enzymes.";
RL Submitted (JAN-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:CCH66847.1}.
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DR EMBL; CAIY01000028; CCH66847.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WYF9; -.
DR STRING; 1165094.RINTHH_6920; -.
DR Proteomes; UP000053051; 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:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyruvate {ECO:0000313|EMBL:CCH66847.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053051};
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 32..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..428
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 860..931
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 942 AA; 104726 MW; E6A86494D1C4E32A CRC64;
MGALPLVSWI VKALTGKQLV HIGTGNISVS AAFYHGGTLA GIAAILSEAS KGIGVVLIAR
AFFGQGTSWE LIALIALVIG RYVVGRGAGT TNVVWGFMVH DPLAATFVFL LASISFIIVR
DRQIAKYGVL LLFPIIELLL HVEDMPRIMA AVILAGLLGW IYSQIPDDFE LSIGEAEQES
QAALKFFRGD YKLLSLDDKL DESRVGHKAA RLSEIRRWGY PVPQGWVLSP YDDPEILIET
LYPSELSPLV VRSSAIGEDS EQASGAGQYE TILNATTRQR LKEAISRVKL SYENPNAVQY
RQSLRLKETA MAVLIQQQIR GVFSGVAFSR DPMTQQGDAV VIEALSGNPN DLVEGKVTPE
QYRAFVVDTA NFSFVQLEGE GKIPAVLIKQ VAYLARHLED KYHGIPQDVE WSFDGQTLWV
LQARPISTLL PIWTRKIAAE VIPGIIHPLT WSINRPLTCG VWGEIFTLVL GRSSSGLDFN
QTAILHYSRA YFNASLLGAI FRRMGLPPES LEFLTRGTKL SKPHLTSTLQ NLSGLLRLFG
KELTLLRDFQ RDEKKYFAPG LSQLAEESID ILEPQDILYR IDSILDLLHH ATYYSIFAPI
SASLRQMLFR VKDSEIDNSF TPEISALKSL NILAASAKVM FPEFDPETLF EDLALSVKGQ
EVLAEFEQWL QKYGYLSEVG TDIAIPTWKE DPCSVKQLFM QIIQRYSSAP NQESCVKTSN
GFVQKRVNLK GKVTETYSRL LAELRWSFIA LEQFWLESGV LSEQGDIFFL ELAEIRLLIE
CNDLELVQGL QSKIRVRRSK REQDSQVQTV PLLVYGNSPS VPIAPSSFYS SQILQGIPAS
HGQVEGRIKV LRNLEFLPEV NQETILVVPY TDSGWTLLLG QVGGLIAEVG GRLSHGAIIA
REYGIPAVMN VHNATSFLKD EQWVRVDGSR GLVEISDDPR PC
//
