ID   A0A0S8IC67_9DELT        Unreviewed;      1398 AA.
AC   A0A0S8IC67;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMJ94_02375 {ECO:0000313|EMBL:KPK93964.1};
OS   Deltaproteobacteria bacterium SM23_61.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK93964.1, ECO:0000313|Proteomes:UP000051218};
RN   [1] {ECO:0000313|EMBL:KPK93964.1, ECO:0000313|Proteomes:UP000051218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_61 {ECO:0000313|EMBL:KPK93964.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK93964.1}.
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DR   EMBL; LJUR01000012; KPK93964.1; -; Genomic_DNA.
DR   STRING; 1703399.AMJ94_02375; -.
DR   PATRIC; fig|1703399.3.peg.2413; -.
DR   Proteomes; UP000051218; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.80.30; -; 1.
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; IPR016024; ARM-type_fold.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR   PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   4: Predicted;
FT   DOMAIN          905..1182
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          1298..1378
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   1398 AA;  160775 MW;  FD79E7FD97E313F3 CRC64;
     MRINLEETAV DQVAVDPKYQ VLREAVSGYR GILKSLDTLL FELHHPYKNW EIILPELRSF
     ALKHFASYSR HPKGPLAVSA MIDVFLDALL NSHKADVEAK AIDHLFSYLE KIVNELNPEN
     RESLLPPLQA CFQDLSSLPE EKFFLLASSH TPLKRIGQVL LRKVSDGSGM SEFNRLMTQS
     LRAAYEYWLK EEDPEEWFAG AVAKPSRQEG QETDLLGEIS HRRFREHLAR LDQISSRDGS
     AETLRDLLEL PGYLEIVRVY REVPQRLAVS AGGDGETLAG NWKILSLFKI MEIPGLRDIH
     EEILREINHT LLALLRKESP ERVGEVLIRT FALLKSNVEN YPQTALQCIQ AIGAEVFKRE
     YSPLVETFLE QVLRFGFQYP GYQGVNANWE IISNPCHVLN VRVWLDIIAR SPKWCSTLLS
     ALIINLRLGG TCIKDTDLFQ KEITKLLNSD IEPVYNLVKQ LTKALPVYFN EIGAEGQLRD
     VTTDIDELRS RKDILIHFLR KQSHVESSNL IEDFIQQIFR FWVRKDKAGL RHFLPLEVFQ
     NLKTEGPFID EVHAILGEIF DRNGLQQEED LLRLSDAEIE EILSSLPSVS DVEKKRVDLL
     VKIYRLINQK YHLGFQEIRY HLQQASRWGF EGLEDLQRIL DRNDTLECLE GILTYLEGLK
     EVIISAQRFE AREDIYRKRH IAVDIPSMYG RYRERKFDAL GLTFRLENLA NVYFERLIDS
     LDLSFITRAT FFQIIRVIDY FFRALQLDGI YSHRLETQLR LLEKSLDIKR FSFTQYLDIF
     RGFSEGVKDI VSVYYLNAHK NNLSNILRQM GRENIQGKFL PPSAEELAPS ELLHQISERF
     LRDLVSTTFG LQYLDNFLTR IHQILAEQRE TLSETDLDLL MTYDAKKVTC FIHKPNPLTN
     DLIHLGGKGY NLVVLASEGI RVPPGFIVTT EVFRCQRIVD RYKYARDHFD REIRAGIQQI
     EKMTGNEFGS TRHPQLLAVR SGATVSMPGM MATLLNVGIN EEIVESMARS TGEVWFAWDN
     YRRFLQSWGM SFGVPREVFS EVMRNFKDRY HVDKKRQFSG EEMKQLALAY RAAVTERHIT
     LYEDPWAQLQ VAIQQVLRSW NSKNARQYRQ IMGISDYWGT AVIVQAMIFG NLGLHSGSGV
     LFTAHPYRKV RRVALWGDFT PGNQGEDIVG GLVTTYPISN EQRQMAGEEG DLSLEQDFPE
     IYKQLFSVSK GLVYDRRWNP QEIEFTYENP DATGLYILQT RDMVSAKRER FEVFLPSPAL
     EESFIGKGIG VSGGALSGRI VFTLEDILRF RRDEPDTPLV LIRSDTVPED VREISLAEGL
     LTAKGGQTSH AAIVAFELDR TAVVGCHSMS VRENEGRCQI NRIPLQRGDW ISLDGRKGLV
     YLGKHEVKDE GEPYHNIL
//