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MULTISPECIES: arabinose-proton symporter AraE [Enterobacteriaceae].


LOCUS       WP_000256438             472 aa            linear   BCT 18-DEC-2020
ACCESSION   WP_000256438
VERSION     WP_000256438.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Ferreira,M.J. and Sa-Nogueira Id.
  TITLE     A multitask ATPase serving different ABC-type sugar importers in
            Bacillus subtilis
  JOURNAL   J. Bacteriol. 192 (20), 5312-5318 (2010)
   PUBMED   20693325
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Mota,L.J., Tavares,P. and Sa-Nogueira,I.
  TITLE     Mode of action of AraR, the key regulator of L-arabinose metabolism
            in Bacillus subtilis
  JOURNAL   Mol. Microbiol. 33 (3), 476-489 (1999)
   PUBMED   10417639
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Krispin,O. and Allmansberger,R.
  TITLE     The Bacillus subtilis AraE protein displays a broad substrate
            specificity for several different sugars
  JOURNAL   J. Bacteriol. 180 (12), 3250-3252 (1998)
   PUBMED   9620981
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Sa-Nogueira,I. and Ramos,S.S.
  TITLE     Cloning, functional analysis, and transcriptional regulation of the
            Bacillus subtilis araE gene involved in L-arabinose utilization
  JOURNAL   J. Bacteriol. 179 (24), 7705-7711 (1997)
   PUBMED   9401028
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Stoner,C. and Schleif,R.
  TITLE     The araE low affinity L-arabinose transport promoter. Cloning,
            sequence, transcription start site and DNA binding sites of
            regulatory proteins
  JOURNAL   J. Mol. Biol. 171 (4), 369-381 (1983)
   PUBMED   6319708
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Daruwalla,K.R., Paxton,A.T. and Henderson,P.J.
  TITLE     Energization of the transport systems for arabinose and comparison
            with galactose transport in Escherichia coli
  JOURNAL   Biochem. J. 200 (3), 611-627 (1981)
   PUBMED   6282256
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR009455
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..472
                     /gene="araE"
     Protein         1..472
                     /product="arabinose-proton symporter AraE"
                     /calculated_mol_wt=51554
     Region          6..457
                     /region_name="SP"
                     /note="MFS transporter, sugar porter (SP) family;
                     TIGR00879"
                     /db_xref="CDD:273317"
     Site            order(36,40,154,157..158,161,269..270,274..275,278..279,
                     307,372..373,376..377,381,404..405,408)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340873"
ORIGIN      
        1 mvtintesal tprslrdtrr mnmfvsvaaa vagllfgldi gviagalpfi tdhfvltsrl
       61 qewvvssmml gaaigalfng wlsfrlgrky slmagailfv lgsigsafat svemliaarv
      121 vlgiavgias ytaplylsem asenvrgkmi smyqlmvtlg ivlaflsdta fsysgnwram
      181 lgvlalpavl liilvvflpn sprwlaekgr hieaeevlrm lrdtsekare elneireslk
      241 lkqggwalfk inrnvrravf lgmllqamqq ftgmniimyy aprifkmagf ttteqqmiat
      301 lvvgltfmfa tfiavftvdk agrkpalkig fsvmalgtlv lgyclmqfdn gtassglswl
      361 svgmtmmcia gyamsaapvv wilcseiqpl kcrdfgitcs tttnwvsnmi igatfltlld
      421 sigaagtfwl ytalniafvg itfwlipetk nvtlehierk lmageklrni gv