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Database: UniProt
Entry: D5UHV0_CELFN
LinkDB: D5UHV0_CELFN
Original site: D5UHV0_CELFN 
ID   D5UHV0_CELFN            Unreviewed;       389 AA.
AC   D5UHV0;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:ADG73374.1};
GN   OrderedLocusNames=Cfla_0459 {ECO:0000313|EMBL:ADG73374.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS   18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG73374.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG73374.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC   NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688; DOI=10.4056/sigs.1012662;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
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DR   EMBL; CP001964; ADG73374.1; -; Genomic_DNA.
DR   RefSeq; WP_013115708.1; NC_014151.1.
DR   AlphaFoldDB; D5UHV0; -.
DR   STRING; 446466.Cfla_0459; -.
DR   KEGG; cfl:Cfla_0459; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG3848; Bacteria.
DR   HOGENOM; CLU_007308_6_0_11; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000000849; Chromosome.
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:ADG73374.1};
KW   Pyruvate {ECO:0000313|EMBL:ADG73374.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000849};
KW   Transferase {ECO:0000313|EMBL:ADG73374.1}.
FT   DOMAIN          45..259
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          312..383
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
SQ   SEQUENCE   389 AA;  39521 MW;  4C6B0A23BAB23D63 CRC64;
     MLVPLPDAVA STCGAKAAHL ATLLRAGLPV PAGVVVPFAR DTDATLRDDL RAALAHLGGG
     PVAVRSSARG EDGADASGAG QHETVLAVRG ADAVLDAVRA CRASLWSPRA RAYREAARSP
     DEPAMAVLVQ RLVDADVAGV AFTPDDPGED VLVDAAWGLG VGVVGGTVTP DAYRLAADGT
     VTCVVADKRT RVDRSGAETV VRDVPTADRA RRTLDEDDVR RIAALARRAA DALGRAQDVE
     WALAGGVPWV LQARPVTAAP PRPPAAGRTG GAAAARPSPA TLVGPLVGTP GSRGTATGPV
     RVVRGPADFA RVRPGDVLVC PWTDPSWTPL LGVVAGVVTE TGGLLSHAAI VARERGVPAV
     LGVTDATRRL RDGALVTLDG AAGTVVPHP
//
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