ID   ARAA_ECOSM              Reviewed;         500 AA.
AC   B1LFZ6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=EcSMS35_0064;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(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;
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   -!- 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; CP000970; ACB18687.1; -; Genomic_DNA.
DR   RefSeq; WP_000151734.1; NC_010498.1.
DR   AlphaFoldDB; B1LFZ6; -.
DR   SMR; B1LFZ6; -.
DR   EnsemblBacteria; ACB18687; ACB18687; EcSMS35_0064.
DR   GeneID; 66671649; -.
DR   KEGG; ecm:EcSMS35_0064; -.
DR   HOGENOM; CLU_045663_0_0_6; -.
DR   OMA; HMLEICP; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000007011; 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.
FT   CHAIN           1..500
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_1000127605"
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   500 AA;  56103 MW;  E1B1B9F2FACF1FBD CRC64;
     MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTTPDEI
     TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF
     MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR
     FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT
     PATQIHGEKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
     YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV
     EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP
     KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT
     RLPAFKDALR WNEVYYGFRR