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Database: UniProt
Entry: A6LBL9_PARD8
LinkDB: A6LBL9_PARD8
Original site: A6LBL9_PARD8 
ID   A6LBL9_PARD8            Unreviewed;       473 AA.
AC   A6LBL9;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Rhamnulose kinase/L-fuculose kinase {ECO:0000313|EMBL:ABR43083.1};
GN   OrderedLocusNames=BDI_1323 {ECO:0000313|EMBL:ABR43083.1};
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR43083.1, ECO:0000313|Proteomes:UP000000566};
RN   [1] {ECO:0000313|EMBL:ABR43083.1, ECO:0000313|Proteomes:UP000000566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC   {ECO:0000313|Proteomes:UP000000566};
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|ARBA:ARBA00009156}.
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DR   EMBL; CP000140; ABR43083.1; -; Genomic_DNA.
DR   RefSeq; WP_009017900.1; NC_009615.1.
DR   AlphaFoldDB; A6LBL9; -.
DR   STRING; 435591.BDI_1323; -.
DR   PaxDb; 435591-BDI_1323; -.
DR   KEGG; pdi:BDI_1323; -.
DR   PATRIC; fig|435591.13.peg.1306; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_039395_0_1_10; -.
DR   OMA; MPDLFNY; -.
DR   BioCyc; PDIS435591:G1G5A-1361-MONOMER; -.
DR   Proteomes; UP000000566; Chromosome.
DR   GO; GO:0008993; F:rhamnulokinase activity; IEA:InterPro.
DR   GO; GO:0019301; P:rhamnose catabolic process; IEA:InterPro.
DR   CDD; cd07771; FGGY_RhuK; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR013449; Rhamnulokinase.
DR   PANTHER; PTHR10196:SF93; L-RHAMNULOKINASE; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABR43083.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000566};
KW   Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..245
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          256..446
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   473 AA;  52979 MW;  5A39FF8A5D56B042 CRC64;
     MKEYNFLAFD IGATSGRAVL GTLKDAKFEM KEIHRFPNPM VELHGRFYWD IYHLYTSLIE
     SLTICARQRI RLHSIGIDTW GVDFGYVALD GSLLGLPRAY RDPYTDGAPE DFFKRIPKEE
     VYKRTGIQVM PFNSLFQLFR AGQDSFIPQE VAEKILFIPD LLAYMLTERM VCEYTIASTS
     QLLNPETHKF DYKLLEAVGV SPTLMCPVVM PGTLIGRLSE SIARKTGIGE IPVIAVAGHD
     TASAVAAVPA SSPNFAYLSS GTWSLMGIEV EKPIINEVSF KNNFTNEGGI EGTTRFLKNI
     TGMWILERCR EQWKRSGLDY SYDDMVRMAE LSEFTSLINP DDPRFANPES MLREITAYCE
     ETGQAVPASD ADYVHCIFYS LANRYKEVLE ILKSMSPHPI ERLHVIGGGS RNDLLNQLTA
     NAIGIPVLAG PSEATAIGNC LIQAKSAGLL TDCWEMRRLI ATAFPPKEFY PER
//
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