ID   ARAA_PHOV8              Reviewed;         509 AA.
AC   A6L2R5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=BVU_2320;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000139; ABR39979.1; -; Genomic_DNA.
DR   RefSeq; WP_011965559.1; NC_009614.1.
DR   AlphaFoldDB; A6L2R5; -.
DR   SMR; A6L2R5; -.
DR   STRING; 435590.BVU_2320; -.
DR   PRIDE; A6L2R5; -.
DR   EnsemblBacteria; ABR39979; ABR39979; BVU_2320.
DR   KEGG; bvu:BVU_2320; -.
DR   PATRIC; fig|435590.9.peg.2395; -.
DR   eggNOG; COG2160; Bacteria.
DR   HOGENOM; CLU_045663_0_0_10; -.
DR   OMA; HMLEICP; -.
DR   OrthoDB; 507566at2; -.
DR   BioCyc; BVUL435590:G1G59-2413-MON; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000002861; 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..509
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_0000312602"
FT   BINDING         313
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         340
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         357
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         456
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ   SEQUENCE   509 AA;  57215 MW;  AED636EE8F09096F CRC64;
     MEKAFDQYEV WFVTGAQLLY GGDAVIAVDA HSNEMVNGLN ESGKLPVKVV YKGTANSSKE
     VEAVFKAANN DEKCIGVITW MHTFSPAKMW IHGLQQLKKP LLHLHTQFNK EIPWDTMDMD
     FMNLNQSAHG DREFGHICTR MRIRRKVVVG YWKDEDTQHK IAVWMRVCAG WADSQDMLII
     RFGDQMNNVA VTDGDKVEAE QRMGYHVDYC PASELMKYHK NIKDTDVEAL VATYFNEYDH
     DASLEDKSTE AYQKVWNAAK AELALRAILK AKGAKGFTTN FDDLGQTDGS YFDQIPGLAS
     QRLMAEGYGF GAEGDWKSAA LYRTVWVMNQ GLSKGCSFLE DYTLNFDGAN SAILQSHMLE
     VCPLIAASKP RLEVHFLGIG IRKSQTARLV FTSKVGSGCT ATVVDLGNRF RLIVNDVECI
     ESKPLPKLPV ASALWIPMPN FEVGAGAWIL AGGTHHSCFS YDLTAEYWED YAEIAGIEMI
     RIDKDTTISN FKKELRMNEV YYMLNKALC