ARAD_BACSU
ID ARAD_BACSU Reviewed; 229 AA.
AC P94525; O05186;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000250|UniProtKB:P08203};
DE EC=5.1.3.4 {ECO:0000250|UniProtKB:P08203};
DE AltName: Full=Phosphoribulose isomerase {ECO:0000250|UniProtKB:P08203};
GN Name=araD; OrderedLocusNames=BSU28780;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9084180; DOI=10.1099/00221287-143-3-957;
RA Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H.;
RT "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence,
RT genetic organization and expression.";
RL Microbiology 143:957-969(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION.
RX PubMed=10417639; DOI=10.1046/j.1365-2958.1999.01484.x;
RA Mota L.J., Tavares P., Sa-Nogueira I.M.G.;
RT "Mode of action of AraR, the key regulator of L-arabinose metabolism in
RT Bacillus subtilis.";
RL Mol. Microbiol. 33:476-489(1999).
CC -!- FUNCTION: Involved in the degradation of L-arabinose. Catalyzes the
CC interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-
CC phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond
CC cleavage analogous to a class II aldolase reaction).
CC {ECO:0000250|UniProtKB:P08203}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226;
CC EC=5.1.3.4; Evidence={ECO:0000250|UniProtKB:P08203};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08203};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08203};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 3/3. {ECO:0000250|UniProtKB:P08203}.
CC -!- INDUCTION: Transcription is repressed by glucose and by the binding of
CC AraR to the operon promoter. L-arabinose acts as an inducer by
CC inhibiting the binding of AraR to the DNA, thus allowing expression of
CC the gene. {ECO:0000269|PubMed:10417639}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000250|UniProtKB:P08203}.
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DR EMBL; X89408; CAA61587.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99589.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14838.1; -; Genomic_DNA.
DR PIR; E69587; E69587.
DR RefSeq; NP_390756.1; NC_000964.3.
DR RefSeq; WP_003229501.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94525; -.
DR SMR; P94525; -.
DR STRING; 224308.BSU28780; -.
DR PaxDb; P94525; -.
DR PRIDE; P94525; -.
DR EnsemblBacteria; CAB14838; CAB14838; BSU_28780.
DR GeneID; 937894; -.
DR KEGG; bsu:BSU28780; -.
DR PATRIC; fig|224308.179.peg.3126; -.
DR eggNOG; COG0235; Bacteria.
DR InParanoid; P94525; -.
DR OMA; PIFGTTH; -.
DR PhylomeDB; P94525; -.
DR BioCyc; BSUB:BSU28780-MON; -.
DR UniPathway; UPA00145; UER00567.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; ISS:UniProtKB.
DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR004661; AraD.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR00760; araD; 1.
PE 2: Evidence at transcript level;
KW Arabinose catabolism; Carbohydrate metabolism; Isomerase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..229
FT /note="L-ribulose-5-phosphate 4-epimerase"
FT /id="PRO_0000162918"
FT ACT_SITE 119
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT ACT_SITE 226
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT BINDING 27..28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT CONFLICT 43..48
FT /note="PSGVEY -> LAESNT (in Ref. 1; CAA61587)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="V -> L (in Ref. 1; CAA61587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 25686 MW; 43F89C216012E2D3 CRC64;
MLETLKKEVL AANLKLQEHQ LVTFTWGNVS GIDREKERIV IKPSGVEYSD LTADDLVVLN
LDGEVVEGSL KPSSDTPTHV YLYKAFPNIG GIVHTHSQWA TSWAQSGRDI PPLGTTHADY
FDSAIPCTRE MYDEEIIHDY ELNTGKVIAE TFQHHNYEQV PGVLVNNHGP FCWGTDALNA
IHNAVVLETV AEMAYHSIML NKDVTPINTV LHEKHFYRKH GANAYYGQS
