ARAA_GEOSE
ID ARAA_GEOSE Reviewed; 496 AA.
AC Q9S467; Q335M1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=L-arabinose isomerase;
DE EC=5.3.1.4;
GN Name=araA;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RA Gilead-Gropper S., Shoham Y.;
RT "The L-arabinose utilization gene cluster from Bacillus stearothermophilus
RT T-6.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=US100;
RX PubMed=16386851; DOI=10.1016/j.bbagen.2005.11.007;
RA Rhimi M., Bejar S.;
RT "Cloning, purification and biochemical characterization of metallic-ions
RT independent and thermoactive L-arabinose isomerase from the Bacillus
RT stearothermophilus US100 strain.";
RL Biochim. Biophys. Acta 1760:191-199(2006).
RN [3]
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF PHE-279; GLU-306; GLU-331; HIS-348 AND
RP HIS-447.
RC STRAIN=US100;
RX PubMed=17337581; DOI=10.1128/jb.01826-06;
RA Rhimi M., Juy M., Aghajari N., Haser R., Bejar S.;
RT "Probing the essential catalytic residues and substrate affinity in the
RT thermoactive Bacillus stearothermophilus US100 L-arabinose isomerase by
RT site-directed mutagenesis.";
RL J. Bacteriol. 189:3556-3563(2007).
CC -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. In
CC vitro, converts D-galactose into D-tagatose.
CC {ECO:0000269|PubMed:16386851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-L-arabinopyranose = L-ribulose; Xref=Rhea:RHEA:14821,
CC ChEBI:CHEBI:16880, ChEBI:CHEBI:40886; EC=5.3.1.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17337581};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:17337581};
CC -!- ACTIVITY REGULATION: Inhibited by copper.
CC {ECO:0000269|PubMed:16386851}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 mM for L-arabinose {ECO:0000269|PubMed:16386851,
CC ECO:0000269|PubMed:17337581};
CC KM=57 mM for D-galactose {ECO:0000269|PubMed:16386851,
CC ECO:0000269|PubMed:17337581};
CC Vmax=41.8 umol/min/mg enzyme with L-arabinose as substrate
CC {ECO:0000269|PubMed:16386851, ECO:0000269|PubMed:17337581};
CC Vmax=8.9 umol/min/mg enzyme with D-galactose as substrate
CC {ECO:0000269|PubMed:16386851, ECO:0000269|PubMed:17337581};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:16386851,
CC ECO:0000269|PubMed:17337581};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:16386851, ECO:0000269|PubMed:17337581};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 1/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16386851}.
CC -!- SIMILARITY: Belongs to the arabinose isomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD45718.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF160811; AAD45718.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ866972; CAI29261.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S467; -.
DR SMR; Q9S467; -.
DR BRENDA; 5.3.1.4; 623.
DR SABIO-RK; Q9S467; -.
DR UniPathway; UPA00145; UER00565.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008733; F:L-arabinose isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10940; -; 1.
DR HAMAP; MF_00519; Arabinose_Isome; 1.
DR InterPro; IPR024664; Ara_Isoase_C.
DR InterPro; IPR038583; AraA_N_sf.
DR InterPro; IPR004216; Fuc/Ara_isomerase_C.
DR InterPro; IPR009015; Fucose_isomerase_N/cen_sf.
DR InterPro; IPR003762; Lara_isomerase.
DR PANTHER; PTHR38464; PTHR38464; 1.
DR Pfam; PF11762; Arabinose_Iso_C; 1.
DR Pfam; PF02610; Arabinose_Isome; 1.
DR PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR SUPFAM; SSF50443; SSF50443; 1.
DR SUPFAM; SSF53743; SSF53743; 1.
PE 1: Evidence at protein level;
KW Arabinose catabolism; Carbohydrate metabolism; Isomerase; Manganese;
KW Metal-binding.
FT CHAIN 1..496
FT /note="L-arabinose isomerase"
FT /id="PRO_0000198381"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MUTAGEN 279
FT /note="F->Q: Increases KM for L-arabinose."
FT /evidence="ECO:0000269|PubMed:17337581"
FT MUTAGEN 306
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17337581"
FT MUTAGEN 331
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17337581"
FT MUTAGEN 348
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17337581"
FT MUTAGEN 447
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17337581"
FT CONFLICT 32..34
FT /note="MMI -> RIM (in Ref. 2; CAI29261)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..40
FT /note="LNQ -> WNR (in Ref. 2; CAI29261)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="L -> F (in Ref. 2; CAI29261)"
FT /evidence="ECO:0000305"
FT CONFLICT 337..339
FT /note="LEP -> FEL (in Ref. 2; CAI29261)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="M -> L (in Ref. 2; CAI29261)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="D -> E (in Ref. 2; CAI29261)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="T -> A (in Ref. 2; CAI29261)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="K -> R (in Ref. 2; CAI29261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 55957 MW; 3542B7B9005A0E41 CRC64;
MLSLRPYEFW FVTGSQHLYG EEALKQVEEH SMMIVNELNQ DSVFPFPLVF KSVVTTPEEI
RRVCLEANAS EQCAGVITWM HTFSPAKMWI GGLLELRKPL LHLHTQFNRD IPWDSIDMDF
MNLNQSAHGD REYGFIGARM GVARKVVVGH WEDPEVRERL AKWMRTAVAF AESRNLKVAR
FGDNMREVAV TEGDKVGAQI QFGWSVNGYG IGDLVQYIRD VSEQKVNELL DEYEELYDIV
PAGRQEGPVR ESIREQARIE LGLKAFLQDG NFTAFTTTFE DLHGMKQLPG LAVQRLMAEG
YGFGGEGDWK TAALVRLMKV MADGKGTSFM EDYTYHLEPG NEMILGAHML EVCPTIAATR
PRIEVHPLSI GGKEDPARLV FDGGEGAAVN ASLIDLGHRF RLIVNEVDAV KPEHDMPKLP
VARILWKPRP SLRDSAEAWI LAGGAHHTCF SFAVTTEQLQ DFAEMAGIEC VVINEHTSVS
SFKNELKWNE VFWRGR
