ID   ARAA_ACIC1              Reviewed;         501 AA.
AC   A0LT86; D2K8A4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Acel_0873;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RA   Cheng L., Mu W., Jiang B.;
RT   "An L-arabinose isomerase from Acidothermus cellulolytics ATCC 43068:
RT   cloning, expression, purification and characterization.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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; GU188440; ACZ67491.1; -; Genomic_DNA.
DR   EMBL; CP000481; ABK52646.1; -; Genomic_DNA.
DR   RefSeq; WP_011719709.1; NC_008578.1.
DR   AlphaFoldDB; A0LT86; -.
DR   SMR; A0LT86; -.
DR   STRING; 351607.Acel_0873; -.
DR   EnsemblBacteria; ABK52646; ABK52646; Acel_0873.
DR   KEGG; ace:Acel_0873; -.
DR   eggNOG; COG2160; Bacteria.
DR   HOGENOM; CLU_045663_0_0_11; -.
DR   OMA; HMLEICP; -.
DR   OrthoDB; 507566at2; -.
DR   BRENDA; 5.3.1.4; 9545.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000008221; 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..501
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_0000312596"
FT   BINDING         307
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         334
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         351
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         450
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ   SEQUENCE   501 AA;  54768 MW;  91128D1CBC0FF35A CRC64;
     MTDLPYPEYE CWFLTGSQHL YGEDVLSAVA RQSQAIVEAL NAAGLPVRLV WKPVLTDATG
     IRRMCSEASA TDACIGVIAW MHTFSPAKAW INGLLALRKP LLHLHTQANL TLPWSTIDMD
     FMNLNQAAHG DREFGYVAAR LAIPRKIVTG HFSDPDVVRD IAAWQRAAAG LADLRSTRLV
     RFGDTMRNVA VTDGDRVEAQ IRLGSAIETY GVHDLGVRVD AVAESDVDAL VDRYLADYDM
     APELTIGGAR HESLRYAAKL ELALRSFLHD GRFTAFTTNF EDLGPLRQLP GIAVQRLMAD
     GFGFGAEGDW KTALLVRAVK TMSRGLPGGT SFMEDYTYHL EPSGRLVLGA HMLEVCPTLT
     SATPRCEIHP LLMGGREDPV RLVFTADPAP AVIVGLCDMG DRLRLVANTA DLVAPPEPLP
     RLPVARAVWQ PHPELKTAAT AWIAAGGPHH TALSTAVSAR EIRDFARMAG LELVLIDEHT
     ALDAALDRLW AIEQTRASRP W