P94525 (ARAD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-ribulose-5-phosphate 4-epimerase
EC=5.1.3.4

Alternative name(s):
Phosphoribulose isomerase

Gene names

Name:	araD
Ordered Locus Names:	BSU28780

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	L-ribulose 5-phosphate = D-xylulose 5-phosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 3/3.
Induction	Transcription is repressed by glucose and by the binding of AraR to the operon promoter. L-arabinose acts as an inducer by inhibiting the binding of AraR to the DNA, thus allowing expression of the gene. Ref.4
Sequence similarities	Belongs to the aldolase class II family. AraD/FucA subfamily.

Ontologies

Keywords
Biological process	Arabinose catabolism Carbohydrate metabolism
Ligand	Metal-binding Zinc
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-arabinose catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	L-ribulose-phosphate 4-epimerase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 229	229	L-ribulose-5-phosphate 4-epimerase		PRO_0000162918
Sites
	Metal binding	94	1	Zinc By similarity
	Metal binding	96	1	Zinc By similarity
	Metal binding	168	1	Zinc By similarity
Experimental info
	Sequence conflict	43 – 48	6	PSGVEY → LAESNT in CAA61587. Ref.1
	Sequence conflict	190	1	V → L in CAA61587. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P94525 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 43F89C216012E2D3	FASTA	229	25,686
	10 20 30 40 50 60 MLETLKKEVL AANLKLQEHQ LVTFTWGNVS GIDREKERIV IKPSGVEYSD LTADDLVVLN 70 80 90 100 110 120 LDGEVVEGSL KPSSDTPTHV YLYKAFPNIG GIVHTHSQWA TSWAQSGRDI PPLGTTHADY 130 140 150 160 170 180 FDSAIPCTRE MYDEEIIHDY ELNTGKVIAE TFQHHNYEQV PGVLVNNHGP FCWGTDALNA 190 200 210 220 IHNAVVLETV AEMAYHSIML NKDVTPINTV LHEKHFYRKH GANAYYGQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression." Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H. Microbiology 143:957-969(1997) [PubMed: 9084180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism." Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R. Microbiology 142:3067-3078(1996) [PubMed: 8969504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis." Mota L.J., Tavares P., Sa-Nogueira I.M.G. Mol. Microbiol. 33:476-489(1999) [PubMed: 10417639] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X89408 Genomic DNA. Translation: CAA61587.1. Z75208 Genomic DNA. Translation: CAA99589.1. AL009126 Genomic DNA. Translation: CAB14838.1.
PIR	E69587.
RefSeq	NP_390756.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P94525.
SMR	P94525. Positions 1-220.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002160; EBBACP00000002160; EBBACG00000002157.
GeneID	937894.
GenomeReviews	Gene locus BSU28780 in contig AL009126_GR.
KEGG	bsu:BSU28780.
NMPDR	fig|224308.1.peg.2881.
PATRIC	18977648. VBIBacSub10457_3012.
Organism-specific databases
GenoList	BSU28780. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002575.
HOGENOM	HBG541069.
OMA	ISCGAEN.
PhylomeDB	P94525.
ProtClustDB	PRK08193.
Enzyme and pathway databases
BioCyc	BSUB:BSU28780-MONOMER.
Family and domain databases
InterPro	IPR001303. Aldolase_II/adducin_N. IPR004661. AraD. [Graphical view]
Gene3D	G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
KO	K01786.
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
SMART	SM01007. Aldolase_II. 1 hit. [Graphical view]
SUPFAM	SSF53639. Aldolase_II_N. 1 hit.
TIGRFAMs	TIGR00760. AraD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARAD_BACSU

Accession

Primary (citable) accession number: P94525
Secondary accession number(s): O05186

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program