ID   U1X2Q5_ANEAE            Unreviewed;       835 AA.
AC   U1X2Q5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Pyruvate phosphate dikinase, PEP/pyruvate binding domain protein {ECO:0000313|EMBL:ERI08813.1};
GN   ORFNames=HMPREF0083_03095 {ECO:0000313|EMBL:ERI08813.1};
OS   Aneurinibacillus aneurinilyticus ATCC 12856.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=649747 {ECO:0000313|EMBL:ERI08813.1, ECO:0000313|Proteomes:UP000016511};
RN   [1] {ECO:0000313|EMBL:ERI08813.1, ECO:0000313|Proteomes:UP000016511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12856 {ECO:0000313|EMBL:ERI08813.1,
RC   ECO:0000313|Proteomes:UP000016511};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) 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:ERI08813.1}.
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DR   EMBL; AWSJ01000189; ERI08813.1; -; Genomic_DNA.
DR   RefSeq; WP_021621941.1; NZ_KE952801.1.
DR   AlphaFoldDB; U1X2Q5; -.
DR   STRING; 649747.HMPREF0083_03095; -.
DR   PATRIC; fig|649747.3.peg.2799; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG3848; Bacteria.
DR   HOGENOM; CLU_005950_0_0_9; -.
DR   Proteomes; UP000016511; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; 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; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ERI08813.1};
KW   Pyruvate {ECO:0000313|EMBL:ERI08813.1};
KW   Transferase {ECO:0000313|EMBL:ERI08813.1}.
FT   DOMAIN          17..305
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          750..821
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   REGION          706..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   835 AA;  94063 MW;  1C8A8C5F315783F0 CRC64;
     MEYITGFDRM LSIEEDGGKG HHLKQLTSFG FNVPEGIVIG ASFYRKYYPK PPVFTYEDEA
     TMASQCQEMA EKVRMTSLPE AFARELEERL ERFPAGGRFA VRSSSTYEDL AGAAFAGQHD
     TFLNIAPDKI AEKVRECFAS LWQKHAVLYR RYQGFEQAGA SMAVVIQRMI EAEVAGVAFS
     VDPVSGNLDY VLIEGNYGVG ESVVGGEAVT DSWIVDAVKG EIVERRVSEK EYYVVPVEDG
     VQTRPLPPEY RATPCLSDDR ILEIARVTKK IEGEFQSPQD VEWAYAENKL YILQSRPQTT
     IPPRFTRDES AERFPEPLTP LTWSYVEDAF NASLEHSLRL MDVHLPTRPW FALRNCYVYG
     NQNAVKLLAM NKPIQLRTAD SLVDELTFIE EKFRWVMELP NTWTRDLDTY LIRVGKLSAA
     SFQGFSATDF QRHFKELFSV AKEYFLPNIA ISMTQGFLTR TLLEYIAVVK GDMYEAQTVL
     KQIITASGTK TGQINRELYE LAKRVKQSPE LMTLLAEGGK QALAGLERFP AFDEAFRVFI
     DNYGHREISF DYYKPTWAEA PEVVLDLIYL AATSRKRENI GKKEQVGKMA SLKATQELLA
     LSPKPLRYFV NELVRLTLTY TYIDDLEHFQ TTRVNLLARK AVGALGNRLM EAGQLADPYD
     LFFLVKEELE SIDSFELSAE LQEKIALRKE AYLRACDQEP VWDLTQESEA ADSEKDAEKD
     GALLRGVPGS PGECEGDIYI VRGPEDFAKM PDQSILVART TNPAWTPLFY KAKGLITESG
     GPLSHGAVTA REVGIPAVMC IRGALTKFEN GERIRLDGKK GVVQKLDVQT KAPMS
//