ARAL_BACSU
ID ARAL_BACSU Reviewed; 272 AA.
AC P94526;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Sugar-phosphatase AraL {ECO:0000303|PubMed:25848029};
DE EC=3.1.3.23 {ECO:0000269|PubMed:21575135, ECO:0000269|PubMed:25848029};
DE AltName: Full=Arabinose operon protein AraL;
DE AltName: Full=Phosphoserine phosphatase {ECO:0000305|PubMed:25848029};
DE EC=3.1.3.3 {ECO:0000269|PubMed:25848029};
GN Name=araL; Synonyms=yseA; OrderedLocusNames=BSU28770;
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 TRANSCRIPTIONAL REGULATION.
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).
RN [5]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21575135; DOI=10.1111/j.1742-4658.2011.08177.x;
RA Godinho L.M., de Sa-Nogueira I.;
RT "Characterization and regulation of a bacterial sugar phosphatase of the
RT haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis.";
RL FEBS J. 278:2511-2524(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
CC -!- FUNCTION: Catalyzes the dephosphorylation of C5 and C6 carbon sugars in
CC vitro (PubMed:21575135, PubMed:25848029). Catalyzes the
CC dephosphorylation of 3'-AMP and phosphoserine in vitro
CC (PubMed:25848029). {ECO:0000269|PubMed:21575135,
CC ECO:0000269|PubMed:25848029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sugar phosphate + H2O = sugar + phosphate.; EC=3.1.3.23;
CC Evidence={ECO:0000269|PubMed:21575135, ECO:0000269|PubMed:25848029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC Evidence={ECO:0000269|PubMed:25848029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC Evidence={ECO:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21575135, ECO:0000269|PubMed:25848029};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29.14 mM for D-xylulose 5-phosphate (at pH 7 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:21575135};
CC KM=24.96 mM for glucose-6-phosphate (at pH 7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21575135};
CC KM=27.36 mM for D-arabinose 5-phosphate (at pH 7 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:21575135};
CC KM=34.89 mM for fructose 6-phosphate (at pH 7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21575135};
CC KM=40.78 mM for fructose 1,6-bisphosphate (at pH 7 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:21575135};
CC KM=40.74 mM for galactose 1-phosphate (at pH 7 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:21575135};
CC KM=50 mM for 4-nitrophenyl phosphate (pNPP) (at pH 7 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:21575135};
CC pH dependence:
CC Optimum pH is 7 with 4-nitrophenyl phosphate as substrate.
CC {ECO:0000269|PubMed:21575135};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius with 4-nitrophenyl
CC phosphate as substrate. {ECO:0000269|PubMed:21575135};
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 HAD-like hydrolase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X89408; CAA61588.1; ALT_INIT; Genomic_DNA.
DR EMBL; X89810; CAA61932.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99590.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14837.1; -; Genomic_DNA.
DR PIR; G69587; G69587.
DR RefSeq; NP_390755.1; NC_000964.3.
DR RefSeq; WP_010886590.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94526; -.
DR SMR; P94526; -.
DR STRING; 224308.BSU28770; -.
DR jPOST; P94526; -.
DR PaxDb; P94526; -.
DR PRIDE; P94526; -.
DR DNASU; 937431; -.
DR EnsemblBacteria; CAB14837; CAB14837; BSU_28770.
DR GeneID; 937431; -.
DR KEGG; bsu:BSU28770; -.
DR PATRIC; fig|224308.43.peg.3011; -.
DR eggNOG; COG0647; Bacteria.
DR InParanoid; P94526; -.
DR OMA; MDGVLIH; -.
DR PhylomeDB; P94526; -.
DR BioCyc; BSUB:BSU28770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0050308; F:sugar-phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13344; Hydrolase_6; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..272
FT /note="Sugar-phosphatase AraL"
FT /id="PRO_0000064658"
SQ SEQUENCE 272 AA; 29315 MW; E035F890C004C51A CRC64;
MRIMASHDTP VSPAGILIDL DGTVFRGNEL IEGAREAIKT LRRMGKKIVF LSNRGNISRA
MCRKKLLGAG IETDVNDIVL SSSVTAAFLK KHYRFSKVWV LGEQGLVDEL RLAGVQNASE
PKEADWLVIS LHETLTYDDL NQAFQAAAGG ARIIATNKDR SFPNEDGNAI DVAGMIGAIE
TSAQAKTELV VGKPSWLMAE AACTAMGLSA HECMIIGDSI ESDIAMGKLY GMKSALVLTG
SAKQGEQRLY TPDYVLDSIK DVTKLAEEGI LI
