(data stored in ACNUC10821 zone)

SWISSPROT: C8U1D3_ECO10

ID   C8U1D3_ECO10            Unreviewed;       500 AA.
AC   C8U1D3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=L-arabinose isomerase {ECO:0000256|HAMAP-Rule:MF_00519, ECO:0000256|SAAS:SAAS00093763};
DE            EC=5.3.1.4 {ECO:0000256|HAMAP-Rule:MF_00519, ECO:0000256|SAAS:SAAS00093763};
GN   Name=araA {ECO:0000256|HAMAP-Rule:MF_00519,
GN   ECO:0000313|EMBL:BAI28941.1};
GN   OrderedLocusNames=ECO103_0063 {ECO:0000313|EMBL:BAI28941.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28941.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28941.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC       {ECO:0000256|HAMAP-Rule:MF_00519, ECO:0000256|SAAS:SAAS00235498}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arabinose = L-ribulose; Xref=Rhea:RHEA:14821,
CC         ChEBI:CHEBI:16880, ChEBI:CHEBI:17535; EC=5.3.1.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00519,
CC         ECO:0000256|SAAS:SAAS01114980};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00519};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00519,
CC       ECO:0000256|SAAS:SAAS00008904}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00519}.
CC   -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00519, ECO:0000256|SAAS:SAAS00538437}.
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DR   EMBL; AP010958; BAI28941.1; -; Genomic_DNA.
DR   RefSeq; WP_000151734.1; NC_013353.1.
DR   SMR; C8U1D3; -.
DR   EnsemblBacteria; BAI28941; BAI28941; ECO103_0063.
DR   KEGG; eoh:ECO103_0063; -.
DR   HOGENOM; HOG000252817; -.
DR   KO; K01804; -.
DR   OMA; HMLEICP; -.
DR   BioCyc; ECOL585395:ECO103_RS00320-MONOMER; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000000959; 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   ProDom; PD018364; Lara_isomerase; 1.
DR   SUPFAM; SSF50443; SSF50443; 1.
DR   SUPFAM; SSF53743; SSF53743; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1D3.
DR   SWISS-2DPAGE; C8U1D3.
KW   Arabinose catabolism {ECO:0000256|HAMAP-Rule:MF_00519,
KW   ECO:0000256|SAAS:SAAS00235475};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00519,
KW   ECO:0000256|SAAS:SAAS00449139};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00519,
KW   ECO:0000256|SAAS:SAAS00068081, ECO:0000313|EMBL:BAI28941.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00519,
KW   ECO:0000256|SAAS:SAAS00449122};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00519,
KW   ECO:0000256|SAAS:SAAS00449118}.
FT   DOMAIN      363    476       Arabinose_Iso_C. {ECO:0000259|Pfam:
FT                                PF11762}.
FT   METAL       306    306       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00519}.
FT   METAL       333    333       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00519}.
FT   METAL       350    350       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00519}.
FT   METAL       450    450       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00519}.
SQ   SEQUENCE   500 AA;  56103 MW;  E1B1B9F2FACF1FBD CRC64;
     MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT 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 MLEVCPSIAV
     EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP
     KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT
     RLPAFKDALR WNEVYYGFRR
//

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