ARAD_ALKHC
ID ARAD_ALKHC Reviewed; 231 AA.
AC Q9KBQ4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=BH1871;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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 -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000250|UniProtKB:P08203}.
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DR EMBL; BA000004; BAB05590.1; -; Genomic_DNA.
DR PIR; G83883; G83883.
DR RefSeq; WP_010898032.1; NC_002570.2.
DR AlphaFoldDB; Q9KBQ4; -.
DR SMR; Q9KBQ4; -.
DR STRING; 272558.10174489; -.
DR EnsemblBacteria; BAB05590; BAB05590; BAB05590.
DR KEGG; bha:BH1871; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_5_0_9; -.
DR OMA; PIFGTTH; -.
DR OrthoDB; 599627at2; -.
DR UniPathway; UPA00145; UER00567.
DR Proteomes; UP000001258; Chromosome.
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 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 3: Inferred from homology;
KW Arabinose catabolism; Carbohydrate metabolism; Isomerase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..231
FT /note="L-ribulose-5-phosphate 4-epimerase"
FT /id="PRO_0000162916"
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"
SQ SEQUENCE 231 AA; 25991 MW; 6CA570D2A6B4DB97 CRC64;
MLEQLKETVF KANLYLPKYQ LVTFTWGNVS GIDREKGLVV IKPSGVEYFE MKSKDMVVVD
LEGNIVEGDL KPSSDTPTHL ALYRAFDKVG GIVHTHSVWA TAWAQAGKEI PAYGTTHADY
FHGTIPCTRP MTETEILGDY EKETGNVIVE TFRNKDPMSI PGVLVHSHAP FVWGKDPMEA
VHHAVVLEEV AKMAQKTLSI SERTLPMDSV LLDRHFYRKH GQAAYYGQEK R