ARAA_LACPL
ID ARAA_LACPL Reviewed; 474 AA.
AC Q88S84; F9ULB0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=L-arabinose isomerase {ECO:0000255|HAMAP-Rule:MF_00519};
DE EC=5.3.1.4 {ECO:0000255|HAMAP-Rule:MF_00519};
GN Name=araA {ECO:0000255|HAMAP-Rule:MF_00519}; OrderedLocusNames=lp_3554;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
CC -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC {ECO:0000255|HAMAP-Rule:MF_00519}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00519};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00519};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00519};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 1/3. {ECO:0000255|HAMAP-Rule:MF_00519}.
CC -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00519}.
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DR EMBL; AL935263; CCC80517.1; -; Genomic_DNA.
DR RefSeq; WP_003642915.1; NC_004567.2.
DR RefSeq; YP_004891031.1; NC_004567.2.
DR AlphaFoldDB; Q88S84; -.
DR SMR; Q88S84; -.
DR STRING; 220668.lp_3554; -.
DR EnsemblBacteria; CCC80517; CCC80517; lp_3554.
DR KEGG; lpl:lp_3554; -.
DR PATRIC; fig|220668.9.peg.2964; -.
DR eggNOG; COG2160; Bacteria.
DR HOGENOM; CLU_045663_0_0_9; -.
DR OMA; REYAFIN; -.
DR PhylomeDB; Q88S84; -.
DR BioCyc; LPLA220668:G1GW0-3005-MON; -.
DR BRENDA; 5.3.1.4; 2849.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000000432; Chromosome.
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 3: Inferred from homology;
KW Arabinose catabolism; Carbohydrate metabolism; Isomerase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..474
FT /note="L-arabinose isomerase"
FT /id="PRO_0000312610"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 447
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ SEQUENCE 474 AA; 53573 MW; 4093B8829B136C49 CRC64;
MLSVPDYEFW FVTGSQHLYG EEQLKSVAKD AQDIADKLNA SGKLPYKVVF KDVMTTAESI
TNFMKEVNYN DKVAGVITWM HTFSPAKNWI RGTELLQKPL LHLATQYLNN IPYADIDFDY
MNLNQSAHGD REYAYINARL QKHNKIVYGY WGDEDVQEQI ARWEDVAVAY NESFKVKVAR
FGDTMRNVAV TEGDKVEAQI KMGWTVDYYG IGDLVEEINK VSDADVDKEY ADLESRYEMV
QGDNDADTYK HSVRVQLAQY LGIKRFLERG GYTAFTTNFE DLWGMEQLPG LASQLLIRDG
YGFGAEGDWK TAALGRVMKI MSHNKQTAFM EDYTLDLRHG HEAILGSHML EVDPSIASDK
PRVEVHPLDI GGKDDPARLV FTGSEGEAID VTVADFRDGF KMISYAVDAN KPEAETPNLP
VAKQLWTPKM GLKKGALEWM QAGGGHHTML SFSLTEEQME DYATMVGMTK AFLK
