ID   ARAA_THEMA              Reviewed;         496 AA.
AC   Q9WYB3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=TM_0276;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD35365.1; -; Genomic_DNA.
DR   PIR; B72398; B72398.
DR   RefSeq; NP_228089.1; NC_000853.1.
DR   RefSeq; WP_004082981.1; NZ_CP011107.1.
DR   PDB; 7CH3; X-ray; 3.61 A; A/B/C/D/E/F/G/H/I/J/K/L=1-496.
DR   PDB; 7CWV; X-ray; 3.53 A; A/B/C/D/E/F/G/H/I/J/K/L=1-496.
DR   PDBsum; 7CH3; -.
DR   PDBsum; 7CWV; -.
DR   AlphaFoldDB; Q9WYB3; -.
DR   SMR; Q9WYB3; -.
DR   STRING; 243274.THEMA_03345; -.
DR   EnsemblBacteria; AAD35365; AAD35365; TM_0276.
DR   KEGG; tma:TM0276; -.
DR   eggNOG; COG2160; Bacteria.
DR   InParanoid; Q9WYB3; -.
DR   OMA; HMLEICP; -.
DR   OrthoDB; 507566at2; -.
DR   BRENDA; 5.3.1.4; 6331.
DR   SABIO-RK; Q9WYB3; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008733; F:L-arabinose isomerase activity; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IBA:GO_Central.
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   3D-structure; Arabinose catabolism; Carbohydrate metabolism; Isomerase;
KW   Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..496
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_0000198394"
FT   BINDING         302
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         329
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         346
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         445
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ   SEQUENCE   496 AA;  56658 MW;  D6AA88752A183DE0 CRC64;
     MIDLKQYEFW FLVGSQYLYG LETLKKVEQQ ASKIVDSLND DPIFPSKIVL KPVLKSSSEI
     TEIFEKANAD PKCAGVIVWM HTFSPSKMWI RGLSINKKPL LHLHTQYNRE IPWDTIDMDY
     MNLNQSAHGD REHGFIHARM RLPRKVVVGH WEEKEVREKI AKWMRVACAI QDGRMGQIVR
     FGDNMREVAS TEGDKVEAQI KLGWSINTWG VGELAERVKA VPEREVEELL KEYREKYIMP
     EDEYSLKAIR EQAKIEIALR EFLKEKNAVG FTTTFEDLHD LPQLPGLAVQ RLMEEGYGFG
     AEGDWKAAGL VRAIKVMGTS LPGGTSFMED YTYHLTPGNE LVLGAHMLEV CPTIAKEKPR
     IEVHPLSIGG KADPARLVFD GQEGPAVNAS IVDMGNRFRL VVNKVLSVPI ERKMPKLPTA
     RVLWKPLPDF KRATTAWILA GGSHHTAFST AIDVEYLIDW AEALEIEYVV IDENLDLEDF
     KKELRWNELY WGLLKR