ID H3SAN4_9BACL Unreviewed; 884 AA.
AC H3SAN4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:EHQ63827.1};
GN ORFNames=PDENDC454_02845 {ECO:0000313|EMBL:EHQ63827.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ63827.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ63827.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ63827.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ63827.1}.
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DR EMBL; AHKH01000005; EHQ63827.1; -; Genomic_DNA.
DR RefSeq; WP_006675075.1; NZ_AHKH01000005.1.
DR AlphaFoldDB; H3SAN4; -.
DR SMR; H3SAN4; -.
DR STRING; 1131935.PDENDC454_02845; -.
DR PATRIC; fig|1131935.3.peg.576; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Pyruvate {ECO:0000313|EMBL:EHQ63827.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900}.
FT DOMAIN 15..311
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 801..872
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT COILED 59..86
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 884 AA; 97685 MW; A66BE8290B8F9213 CRC64;
MNCVNLDRVN RTHLPLAGGK GANLGELRQA GFPVPPGFCV TTSVYDAVVG QSDRMDSFYE
ELGLLNVQAN EEIRRLSQRM QRHISSLPIP DEMIEDILGA WREMGDNPVA AVRSSATAED
LPTASFAGQQ DTLLNVKGER QLFEAIRQCW SSLFSERAIA YRMKNGFDHR SVRLAVIVQR
LIVPDVSGVM FTADPITGNR SIISIDASFG LGEALVSGLV NPDLYQVRQG EIVKKQISCK
KSAVCTLAEG GTAVEELPEP KQKEQALSDE QIVTLARMGE RIQAHYGAEQ DIEWCLSGGQ
FYIVQARPIT SIFPLPQAPD DGLHVYFSFG HMQMMTDAMS PAGISVWQMT RDFAAAGEER
AAALVEAGGR LFMDATRSLQ AGLARKVTLQ MIGKMDALIA SAARQILDRF PLKEKSSSGW
EGLEEMLPRL ATQVLKDMLE GEGQAAYTEV EDGADHLVDK CRQRLDECDG ADKITYIHQN
YESLARYLMG ESFHYMVTAM VAQHLLELLA KWWNFDGGEL ITLNKSLPFN VTSEMGLELG
DVADTARPYP ELTAYLRNAA EDGFMEGLDA IAGGPEFKAA FARWLERYGV RCPGEIDIMR
TRWGERPYML IPSIVGHLDS LQHGEHRERF RQGEQEAERA AGRILSQVRG LEDGAFKERI
VSRLITVYRS FMGLREHHKF VLVRHLALYR KAVLELGDDL AAQGVLSERN EMFFLALPEM
KEIITGTFAE DVPSLIAARK ESFKHYQRLQ PPRVFTSEGE IIEGRLDGGD APEGALIGLP
VSPGVVEGRA RIVLDPSTAS LKEGEILVAP FTDPGWTPLF QQARGLITEI GGMMTHGSVV
AREYGIPAIV GVERATKLIR DGELLRLDGT TGHVIVLEEA HSLA
//
