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
//