(data stored in ACNUC7421 zone)

SWISSPROT: D6XWP1_BACIE

ID   D6XWP1_BACIE            Unreviewed;       492 AA.
AC   D6XWP1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 62.
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   OrderedLocusNames=Bsel_0343 {ECO:0000313|EMBL:ADH97883.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97883.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97883.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00519, ECO:0000256|SAAS:SAAS00538437}.
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DR   EMBL; CP001791; ADH97883.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0343; -.
DR   EnsemblBacteria; ADH97883; ADH97883; Bsel_0343.
DR   KEGG; bse:Bsel_0343; -.
DR   eggNOG; ENOG4105CAC; Bacteria.
DR   eggNOG; COG2160; LUCA.
DR   HOGENOM; HOG000252817; -.
DR   KO; K01804; -.
DR   OMA; HMLEICP; -.
DR   BioCyc; BSEL439292:G1GLR-368-MONOMER; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000000271; 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; D6XWP1.
DR   SWISS-2DPAGE; D6XWP1.
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:UP000000271};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00519,
KW   ECO:0000256|SAAS:SAAS00068081, ECO:0000313|EMBL:ADH97883.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN      358    471       Arabinose_Iso_C. {ECO:0000259|Pfam:
FT                                PF11762}.
FT   METAL       304    304       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00519}.
FT   METAL       329    329       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00519}.
FT   METAL       346    346       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00519}.
FT   METAL       445    445       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_00519}.
SQ   SEQUENCE   492 AA;  55113 MW;  E86407F874C46CA3 CRC64;
     MINRPYSFWF LTGSQHLYGP ETLDQVAAQS EEIIDGLNEA GLPFPIEAKQ VLTNSDDIRD
     VIIAANADPS CAGVITWMHT FSPSKIWIRG LQLLQKPMLH LNTQHNRDIP WDQIDMDFMN
     LNQSAHGDRE FGSVVTRLGI DRKVVVGHWQ HPDVQADISS WMVTAMGHQE SYHVKVARFG
     DNMRRVAVTD GDKVEAQNVF GWTVDGFGVG DLVAYIDKVT DEETESLFDE YDKLYRISDE
     IKQTPALKQS VLEQARIELG MKAFLDTEGY NAFTTTFEDL HGMKQLPGLA AQRLMAQGYG
     FAGEGDWKTA ALLRLMKVMA GHEQTTFMED YTYHFEPDNE MVLGSHMLEV CPTVAEDKPE
     IKVHPLGIGG KDDPARLVFN GQGGKGVNVS LVDIGTRFRL IISEVEAQVP DKETPELPVA
     KLLWKPEPSL STATAAWVHA GGAHHTVLTF SLTVDQMLDW AEMHGIEAAV INGETDIHQF
     KKELKWNELV WK
//

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