ID A0A1F5B8G3_9BACT Unreviewed; 371 AA.
AC A0A1F5B8G3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU364073};
DE Short=Xylulokinase {ECO:0000256|RuleBase:RU364073};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU364073};
DE Flags: Fragment;
GN Name=xylB {ECO:0000256|RuleBase:RU364073};
GN ORFNames=A2028_02340 {ECO:0000313|EMBL:OGD26879.1};
OS Candidatus Aminicenantes bacterium RBG_19FT_COMBO_59_29.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797276 {ECO:0000313|EMBL:OGD26879.1, ECO:0000313|Proteomes:UP000179239};
RN [1] {ECO:0000313|EMBL:OGD26879.1, ECO:0000313|Proteomes:UP000179239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216;
CC EC=2.7.1.17; Evidence={ECO:0000256|RuleBase:RU364073};
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|RuleBase:RU364073}.
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:OGD26879.1}.
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DR EMBL; MEYE01000083; OGD26879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5B8G3; -.
DR Proteomes; UP000179239; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005997; P:xylulose metabolic process; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR006000; Xylulokinase.
DR NCBIfam; TIGR01312; XylB; 1.
DR PANTHER; PTHR43095; SUGAR KINASE; 1.
DR PANTHER; PTHR43095:SF5; XYLULOSE KINASE; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364073};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU364073};
KW Kinase {ECO:0000256|RuleBase:RU364073, ECO:0000313|EMBL:OGD26879.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364073};
KW Transferase {ECO:0000256|RuleBase:RU364073};
KW Xylose metabolism {ECO:0000256|RuleBase:RU364073}.
FT DOMAIN 2..248
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT NON_TER 371
FT /evidence="ECO:0000313|EMBL:OGD26879.1"
SQ SEQUENCE 371 AA; 40078 MW; 4ABDC2A5D2399B90 CRC64;
MYAIGIDSGT QGTKALVVDF KGKVRGRGYA PHLSVPNLKP GESEQHPQAW VEATQKAMTA
ALTESKVNPK KIVSLGVSGQ QHGFVPLDKS GRPVRPAKLW NDTSTIPETE FIIDKLGGKK
SYIKKLGINL AVGFTASKIL WLKRQEPKNF ERTISVLLPH NYLNFWISGK AVMEFGDASG
TGLMDIRRRV WHREAIAAID PALEAKLPPL RHPAEPIGLV ERQVASRYGM GHVLVSSGGG
DNMMGAIGTG NVSPGICTAS LGTSGTIYSF FREPFVDPEG EIAAFCDSTG GWLPLLCTMN
VTNTTEFFKS MHGLSNQELE TLASRAPAGA DGLIFLPFID GERIPVLPHS SGVLFGLNKR
TFNAAHFARA I
//
