GenomeNet

Database: UniProt
Entry: A0A101VAR0_9FIRM
LinkDB: A0A101VAR0_9FIRM
Original site: A0A101VAR0_9FIRM 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system