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Database: UniProt
Entry: F2JNR9_CELLD
LinkDB: F2JNR9_CELLD
Original site: F2JNR9_CELLD 
ID   F2JNR9_CELLD            Unreviewed;       425 AA.
AC   F2JNR9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=HAD-superfamily hydrolase, subfamily IA, variant 1 {ECO:0000313|EMBL:ADZ82417.1};
GN   OrderedLocusNames=Clole_0684 {ECO:0000313|EMBL:ADZ82417.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ82417.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ82417.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
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DR   EMBL; CP002582; ADZ82417.1; -; Genomic_DNA.
DR   RefSeq; WP_013655718.1; NC_015275.1.
DR   AlphaFoldDB; F2JNR9; -.
DR   STRING; 642492.Clole_0684; -.
DR   KEGG; cle:Clole_0684; -.
DR   eggNOG; COG0546; Bacteria.
DR   eggNOG; COG0572; Bacteria.
DR   HOGENOM; CLU_645106_0_0_9; -.
DR   Proteomes; UP000008467; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR006083; PRK/URK.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   PANTHER; PTHR43434:SF1; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G00760)-RELATED; 1.
DR   PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   Pfam; PF13419; HAD_2; 1.
DR   Pfam; PF00485; PRK; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ADZ82417.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467}.
FT   DOMAIN          220..369
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
SQ   SEQUENCE   425 AA;  48685 MW;  37EDB5B31FC30D5F CRC64;
     MIIIFDLDGT LFQTALCDIA AVNHLFDELA IEKVDDTAIT YNIGKKTFEF LTNILPPHIK
     QQDVYDRFRE LEQKEVRENG ILFPGVIELL EELVSKGHTL IICSNGSSEY IELVLKKTGI
     TKYFSNIYSA KEANNKGEVI RKILDNNSPA VVIGDTLSDI EAAAENNIPS IAAMYGYGNI
     NELGAATYII QNVTDIIGYV NRIEIFYAIT DRSIRKGKKV IGINGVDTSG KTVFTKAYSK
     FLSSLKIKNT IIHIDDYHNP AELRCKGDNE IEAYYHNAFN YDQVIDEILG PLSELKSINK
     DVLCLNLDTN KYENFIHYNI DENTIVLIEG VLLFREPLLK YLDTTVFLHI DFDEVLRRMQ
     VRDVPKYGEG FIKKYANKYI PVQRKYLEEY RPEQRSDIVI NNQDYFNPRL GAYCEGKDDI
     YNNRK
//
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