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Database: UniProt
Entry: Q8RMB9_THENE
LinkDB: Q8RMB9_THENE
Original site: Q8RMB9_THENE 
ID   Q8RMB9_THENE            Unreviewed;       496 AA.
AC   Q8RMB9;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   11-JUN-2014, entry version 46.
DE   RecName: Full=L-arabinose isomerase;
DE            EC=5.3.1.4;
GN   Name=araA;
OS   Thermotoga neapolitana.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=2337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Kim B.-C., Lee Y.-H., Lee D.-W., Lee H.-S., Jang H.-J., Pyun Y.-R.;
RT   "Cloning, sequencing, and expression in Escherichia coli of a
RT   thermophilic Arabinose isomerase from Thermotoga neapolitana.";
RL   Submitted (MAR-2001) 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   -!- SIMILARITY: Belongs to the arabinose isomerase family.
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DR   EMBL; AY028379; AAK18729.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8RMB9; -.
DR   SMR; Q8RMB9; 1-493.
DR   SABIO-RK; Q8RMB9; -.
DR   UniPathway; UPA00145; UER00565.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008733; F:L-arabinose isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-HAMAP.
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; SSF50443; 1.
DR   SUPFAM; SSF53743; SSF53743; 1.
PE   3: Inferred from homology;
KW   Arabinose catabolism; Carbohydrate metabolism; Isomerase; Manganese;
KW   Metal-binding.
FT   METAL       302    302       Manganese (By similarity){EA2}.
FT   METAL       329    329       Manganese (By similarity){EA2}.
FT   METAL       346    346       Manganese (By similarity){EA2}.
FT   METAL       445    445       Manganese (By similarity){EA2}.
SQ   SEQUENCE   496 AA;  56677 MW;  531EEBEC1042BA93 CRC64;
     MIDLKQYEFW FLVGSQYLYG LETLKKVEQQ ASRIVEALNN DPIFPSKIVL KPVLKNSAEI
     REIFEKANAE PKCAGVIVWM HTFSPSKMWI RGLSINKKPL LHLHTQYNRE IPWDTIDMDY
     MNLNQSAHGD REHGFIHARM RLPRKVVVGH WEDREVREKI AKWMRVACAI QDGRTGQIVR
     FGDNMREVAS TEDDKVEAQI KLGWSINTWG VGELAEGVKA VPENEVEELL KEYKERYIMP
     EDEYSLKAIR EQAKMEIALR EFLKEKNAIA FTTTFEDLHD LPQLPGLAVQ RLMEEGYGFG
     AEGDWKAAGL VRALKVMGAG LPGGTSFMED YTYHLTPGNE LVLGAHMLEV CPTIAKEKPR
     IEVHPLSIGG KADPARLVFD GQEGPAVNAS IVDMGNRFRL VVNRVLSVPI ERKMPKLPTA
     RVLWKPLPDF KRATTAWILA GGSHHTAFST AVDVEYLIDW AEALEIEYLV IDENLDLENF
     KKELRWNELY WGLLKR
//
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