(data stored in ACNUC7421 zone)

SWISSPROT: ARAA_ECO57

ID   ARAA_ECO57              Reviewed;         500 AA.
AC   P58538;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   05-JUL-2017, entry version 91.
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};
GN   OrderedLocusNames=Z0070, ECs0066;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC       {ECO:0000255|HAMAP-Rule:MF_00519}.
CC   -!- CATALYTIC ACTIVITY: L-arabinose = L-ribulose. {ECO:0000255|HAMAP-
CC       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-
CC       Rule:MF_00519};
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial
CC       route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_00519}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00519}.
CC   -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00519}.
DR   EMBL; AE005174; AAG54366.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33489.1; -; Genomic_DNA.
DR   PIR; B85488; B85488.
DR   PIR; B90637; B90637.
DR   RefSeq; NP_308093.1; NC_002695.1.
DR   RefSeq; WP_000151715.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; P58538; -.
DR   SMR; P58538; -.
DR   STRING; 155864.Z0070; -.
DR   EnsemblBacteria; AAG54366; AAG54366; Z0070.
DR   EnsemblBacteria; BAB33489; BAB33489; BAB33489.
DR   GeneID; 913468; -.
DR   KEGG; ece:Z0070; -.
DR   KEGG; ecs:ECs0066; -.
DR   PATRIC; fig|386585.9.peg.166; -.
DR   eggNOG; ENOG4105CAC; Bacteria.
DR   eggNOG; COG2160; LUCA.
DR   HOGENOM; HOG000252817; -.
DR   KO; K01804; -.
DR   BRENDA; 5.3.1.4; 2026.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008733; F:L-arabinose isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; SSF50443; 1.
DR   SUPFAM; SSF53743; SSF53743; 1.
PE   3: Inferred from homology;
DR   PRODOM; P58538.
DR   SWISS-2DPAGE; P58538.
KW   Arabinose catabolism; Carbohydrate metabolism; Complete proteome;
KW   Isomerase; Manganese; Metal-binding.
FT   CHAIN         1    500       L-arabinose isomerase.
FT                                /FTId=PRO_0000198387.
FT   METAL       306    306       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00519}.
FT   METAL       333    333       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00519}.
FT   METAL       350    350       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00519}.
FT   METAL       450    450       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00519}.
SQ   SEQUENCE   500 AA;  56089 MW;  9267F72676A53EE0 CRC64;
     MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVKALNT EAKLPCKLVL KPLGTTPDEI
     TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF
     MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR
     FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT
     PATQIHGEKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
     YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAA
     EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP
     KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT
     RLPAFKDALR WNEVYYGFRR
//

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