ID   ARAA_ERWT9              Reviewed;         501 AA.
AC   B2VER0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   28-JAN-2026, entry version 82.
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};
GN   OrderedLocusNames=ETA_17720;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; Evidence={ECO:0000255|HAMAP-
CC         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   -!- SUBUNIT: Homohexamer. {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; CU468135; CAO96818.1; -; Genomic_DNA.
DR   RefSeq; WP_012441507.1; NC_010694.1.
DR   AlphaFoldDB; B2VER0; -.
DR   SMR; B2VER0; -.
DR   STRING; 465817.ETA_17720; -.
DR   KEGG; eta:ETA_17720; -.
DR   eggNOG; COG2160; Bacteria.
DR   HOGENOM; CLU_045663_0_0_6; -.
DR   OrthoDB; 9765600at2; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000001726; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 D-xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR   CDD; cd03557; L-arabinose_isomerase; 1.
DR   Gene3D; 3.40.50.10940; -; 1.
DR   HAMAP; MF_00519; Arabinose_Isome; 1.
DR   InterPro; IPR024664; Ara_Isoase_C.
DR   InterPro; IPR055390; AraA_central.
DR   InterPro; IPR055389; AraA_N.
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   NCBIfam; NF002795; PRK02929.1; 1.
DR   PANTHER; PTHR38464; L-ARABINOSE ISOMERASE; 1.
DR   PANTHER; PTHR38464:SF1; L-ARABINOSE ISOMERASE; 1.
DR   Pfam; PF24856; AraA_central; 1.
DR   Pfam; PF02610; AraA_N; 1.
DR   Pfam; PF11762; Arabinose_Iso_C; 1.
DR   PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR   SUPFAM; SSF50443; FucI/AraA C-terminal domain-like; 1.
DR   SUPFAM; SSF53743; FucI/AraA N-terminal and middle domains; 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_1000127606"
FT   BINDING         306
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         333
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         350
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;  55549 MW;  98E1368865BEED5B CRC64;
     MTQINNRSVW FVIGTQHLYG VETLRQVERH GQQVVDSLNR SGILPFRLQI RPLVKTPDEA
     LALCREANYD SECYGIMTWL HTFSPAKMWI GGLSVLHKPL LQFHTQFNAE IPWDSMDMDF
     MNLNQTAHGG REFGFIGARM RLPHQVVTGH WQDERTLLRI GQWMRTAAAL QAGRQLKVAR
     FGDNMREVAV TEGDKVAAQI QFGYSVNGWG VGDLVEVINQ VKDGDVNALV DEYESRYVFS
     AAAAVGGAKR QNVLDAARIE LGIGRFLDDE GCRAFTTNFQ TLHGMTQLPG LAVQRLMQQG
     YGFAGEGDWK TAALLHICKV MAGDLTGGTS FMEDYTYHFA PDNDLVLGSH MLEVCPSIAS
     EARPLLDVQP LGIGGKADPA RLIFAAKAGR AVNASVIDMG DRFRLLVNVL DAVEPPRALP
     KLPVARALWH AQPSLATASE AWILGGGAHH TVFSQALTVD DLRLYGEMLG IEVVVIDEQT
     TLHGLRDALR WNEAYYRLNQ R
//