ID A0A101VAR0_9FIRM Unreviewed; 864 AA.
AC A0A101VAR0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=APF76_16920 {ECO:0000313|EMBL:KUO51173.1};
OS Desulfitibacter sp. BRH_c19.
OC Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC Desulfitibacter.
OX NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO51173.1, ECO:0000313|Proteomes:UP000053015};
RN [1] {ECO:0000313|EMBL:KUO51173.1, ECO:0000313|Proteomes:UP000053015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO51173.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO51173.1}.
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DR EMBL; LOER01000026; KUO51173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VAR0; -.
DR STRING; 1734395.APF76_16920; -.
DR Proteomes; UP000053015; 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;
FT DOMAIN 20..315
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 787..858
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 864 AA; 97173 MW; 2CDBBC4A2F5EB55C CRC64;
MSQLNYVKSL KDITRRDFEN VGGKGANLGE MIQAGLPVPE GFVVQTSAYR DFIKESNLNE
RINSLVTNLE ANDIEVLENV SEMINKLFQD CSIPKRILDE INAVYENLYG IPVAIRSSAT
AEDLPGTSFA GQYDTFLNIT GIDNVYVAIK KCWASLWNAR ALSYRLKYNV PNDELAHGVV
VQKLVSGEKS GILFTANPLN DRRDQMLINA SRGLGEAIVG GEVTPDQWTI KSATGSIEEV
RISIKEFMTV KEDGGTCTKK VPEELQNKPV LNEEEIKALV EFGRKTEQYF GCPQDIEWTL
NEGIIYLVQS RPITSLFPMP TSDTDSDNTL RIYLNFNLIG QGLTEPFTPM GQEIWRLIFS
GYTKIATGKE DVNYPIWFKV IAGRIFIDMT DLMRKKKAWN KSANTLSTKD PVTSKALLQW
LEKNEQEILK GNRIKFSAHL IKVVVSLVGD FVYGMLLPQK ARKKVIEIGN KHIDILRKQA
DSLIRIEDKL RFIEKNGKDI TLIGFKKMAY IGFGLRAIDK AESLLIKWNI DTAGIDRIKQ
SLPYNVTTEM GLELLEIAEC SKGENLEQFI KHPDIERFMK KYGHRAVTEI DVGMDRWRED
PSYVIDLIKS YREHGDSKDK IKKFSNGMVK ADMAIEEFVA SVRKRKGRGA ANKIKGLLQS
YREVAGLREQ PKYDIVRTID IFRDILLSIG KELAILSRLE KAEDVFYITF KDIESGMPLH
EIVLENKDTY QKELKRKSTP RLVASTGESI YSINEEEGPN TFVGIPVSPG VYEGKVRIIE
KLKDAQLKKG EILVTRGTDP AWTPLFLNAG AIIMESGGPL SHGTVVAREY GIPAVVGIRN
ACTRLKNSQI VRVNGESGQI VIMG
//