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Database: UniProt/SWISS-PROT
Entry: ARAA_SALSV
LinkDB: ARAA_SALSV
Original site: ARAA_SALSV 
ID   ARAA_SALSV              Reviewed;         500 AA.
AC   B4TWU8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   01-MAY-2013, entry version 32.
DE   RecName: Full=L-arabinose isomerase;
DE            EC=5.3.1.4;
GN   Name=araA; OrderedLocusNames=SeSA_A0113;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RA   Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M.,
RA   Leclerc J., Cebula T., Sebastian Y.;
RT   "Complete genome of Salmonella schwarzengrund strain CVM19633.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-arabinose = L-ribulose.
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial
CC       route): step 1/3.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SIMILARITY: Belongs to the arabinose isomerase family.
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DR   EMBL; CP001127; ACF90120.1; -; Genomic_DNA.
DR   RefSeq; YP_002113119.1; NC_011094.1.
DR   ProteinModelPortal; B4TWU8; -.
DR   STRING; 439843.SeSA_A0113; -.
DR   EnsemblBacteria; ACF90120; ACF90120; SeSA_A0113.
DR   GeneID; 6517583; -.
DR   KEGG; sew:SeSA_A0113; -.
DR   PATRIC; 32368909; VBISalEnt87589_0232.
DR   eggNOG; COG2160; -.
DR   HOGENOM; HOG000252817; -.
DR   KO; K01804; -.
DR   OMA; KPLLHLH; -.
DR   ProtClustDB; PRK02929; -.
DR   BioCyc; SENT439843:GHHR-1546-MONOMER; -.
DR   UniPathway; UPA00145; UER00565.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008733; F:L-arabinose isomerase activity; IEA:HAMAP.
DR   GO; GO:0008736; F:L-fucose isomerase activity; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR   GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00519; Arabinose_Isome; 1; -.
DR   InterPro; IPR024664; Ara_Isoase_C.
DR   InterPro; IPR004216; Fuc/Ara_isomerase_C.
DR   InterPro; IPR009015; Fucose_isomerase_N/cen.
DR   InterPro; IPR003762; Lara_isomerase.
DR   Pfam; PF11762; Arabinose_Iso_C; 1.
DR   Pfam; PF02610; Arabinose_Isome; 1.
DR   PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR   ProDom; PD018364; Lara_isomerase; 1.
DR   SUPFAM; SSF50443; Fuc_isomerase_C; 1.
DR   SUPFAM; SSF53743; Fuc_isomerase_N; 1.
PE   3: Inferred from homology;
KW   Arabinose catabolism; Carbohydrate metabolism; Complete proteome;
KW   Isomerase; Manganese; Metal-binding.
FT   CHAIN         1    500       L-arabinose isomerase.
FT                                /FTId=PRO_1000127619.
FT   METAL       306    306       Manganese (By similarity).
FT   METAL       333    333       Manganese (By similarity).
FT   METAL       350    350       Manganese (By similarity).
FT   METAL       450    450       Manganese (By similarity).
SQ   SEQUENCE   500 AA;  55969 MW;  96A8B71F11C1C478 CRC64;
     MTIFDNYEVW FVIGSQHLYG AETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTSPDEI
     TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLSILNKPL LQFHTQFNAA LPWDSIDMDF
     MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKEAHTRI GAWMRQAVSK QDTRQLKVCR
     FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDINALI DEYESSYTLT
     PATRIHGDKR QNVREAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
     YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV
     EEKPILDVQH LGIGGKEDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP
     KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALDLN DMRQFAEIHD IEIAVIDNDT
     RLPAFKDALR WNEVYYGFKR
//
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