ID B2IC59_BEII9 Unreviewed; 531 AA.
AC B2IC59;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding {ECO:0000313|EMBL:ACB96656.1};
GN OrderedLocusNames=Bind_3095 {ECO:0000313|EMBL:ACB96656.1};
OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS 8712).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Beijerinckia.
OX NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB96656.1, ECO:0000313|Proteomes:UP000001695};
RN [1] {ECO:0000313|Proteomes:UP000001695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC {ECO:0000313|Proteomes:UP000001695};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT 9039.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB96656.1, ECO:0000313|Proteomes:UP000001695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC {ECO:0000313|Proteomes:UP000001695};
RX PubMed=20601475; DOI=10.1128/JB.00656-10;
RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA Dunfield P.F.;
RT "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL J. Bacteriol. 192:4532-4533(2010).
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DR EMBL; CP001016; ACB96656.1; -; Genomic_DNA.
DR RefSeq; WP_012386004.1; NC_010581.1.
DR AlphaFoldDB; B2IC59; -.
DR STRING; 395963.Bind_3095; -.
DR KEGG; bid:Bind_3095; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_2_0_5; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000001695; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
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; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACB96656.1};
KW Pyruvate {ECO:0000313|EMBL:ACB96656.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001695};
KW Transferase {ECO:0000313|EMBL:ACB96656.1}.
FT DOMAIN 61..287
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 299..343
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 420..501
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 531 AA; 56221 MW; D4F9A7A36FDAAC79 CRC64;
MQIVRIATGT NEAHSADLIG AKAANLERMA ALGLPVPPAF VLPITLCSAI LRSEPEAEKA
LVKGLEEGIA YLEEATGRRF GDHRHPLLIS VRSGAARSMP GMLETVLDVG CTPSVVLGLV
RQTGHPRFAW DCRCRFLDSY ADVVLGLDQA LLRKRRDQIM AEEGVLDAGD LDSEALERLA
GAYLQVIESN GGFIPEEPMR QVEAAARMVF GSWESDKAKT YRKLEHLEAL GGTAVTVQAM
VFGNVGLTSG AGVAFSRDPS TGAATPVIDV LFESQGEDVV SGRRTPEPEA ALARTVPAAA
KELVATLARL EQAFGDVQDV EFTIENGKLW FLQTRSAKRT PAAALRFAVA FVKEGLITPK
EALQRLENID FTRDIEHLAN QRLSAVGEPV GHGTGASTGV AIGRAAFDST SAQRLAKAGD
PVILLRPEIS TADVAGFAAS AGIVTAVGGR TAHAALVARQ LGKPCLVGCA GLNVDVAGHT
ARLHDLPIKE GDWLSIDGGA GTIFSGRGKL LIDRPEAELS EIARWKESVP A
//
