ARAA_ECOLI
ID ARAA_ECOLI Reviewed; 500 AA.
AC P08202; P78040;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=L-arabinose isomerase;
DE EC=5.3.1.4;
GN Name=araA; OrderedLocusNames=b0062, JW0061;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3549454; DOI=10.1016/0378-1119(86)90067-3;
RA Lee N., Gielow W., Martin R., Hamilton E., Fowler A.;
RT "The organization of the araBAD operon of Escherichia coli.";
RL Gene 47:231-244(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 72;
RP 248 AND 360.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 458-500.
RA Bachellier S., Saurin W., Perrin D., Hofnung M., Gilson E.;
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION.
RX PubMed=328165; DOI=10.1016/0092-8674(77)90072-1;
RA Hirsh J., Schleif R.;
RT "The araC promoter: transcription, mapping and interaction with the araBAD
RT promoter.";
RL Cell 11:545-550(1977).
RN [7]
RP INDUCTION.
RX PubMed=2962192; DOI=10.1073/pnas.84.24.8814;
RA Lee N., Francklyn C., Hamilton E.P.;
RT "Arabinose-induced binding of AraC protein to araI2 activates the araBAD
RT operon promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8814-8818(1987).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=16756997; DOI=10.1016/j.jmb.2006.04.040;
RA Manjasetty B.A., Chance M.R.;
RT "Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the
RT putative target of biological tagatose production.";
RL J. Mol. Biol. 360:297-309(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS.
RA Zhu W., Chance M.R., Manjasetty B.A.;
RT "Crystal structure of Mn2+-bound Escherichia coli L-arabinose isomerase
RT (ECAI) and implications in protein catalytic mechanism and thermo-
RT stability.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-L-arabinopyranose = L-ribulose; Xref=Rhea:RHEA:14821,
CC ChEBI:CHEBI:16880, ChEBI:CHEBI:40886; EC=5.3.1.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 1 Mn(2+) ion per subunit.;
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 1/3.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:16756997,
CC ECO:0000269|Ref.10}.
CC -!- INDUCTION: Induced by arabinose. Transcription is dependent on the
CC transcription factor AraC, the cAMP receptor protein (CRP) and cAMP.
CC {ECO:0000269|PubMed:2962192, ECO:0000269|PubMed:328165}.
CC -!- SIMILARITY: Belongs to the arabinose isomerase family. {ECO:0000305}.
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DR EMBL; M15263; AAA23463.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73173.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96631.2; -; Genomic_DNA.
DR EMBL; X74279; CAA52340.1; -; Genomic_DNA.
DR PIR; F64727; ISECAB.
DR RefSeq; NP_414604.1; NC_000913.3.
DR RefSeq; WP_000151748.1; NZ_SSZK01000004.1.
DR PDB; 2AJT; X-ray; 2.60 A; A/B/C=1-500.
DR PDB; 2HXG; X-ray; 2.80 A; A/B/C=1-500.
DR PDB; 4F2D; X-ray; 2.30 A; A/B/C=1-500.
DR PDB; 7CHL; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L=285-382.
DR PDBsum; 2AJT; -.
DR PDBsum; 2HXG; -.
DR PDBsum; 4F2D; -.
DR PDBsum; 7CHL; -.
DR AlphaFoldDB; P08202; -.
DR SMR; P08202; -.
DR BioGRID; 4259464; 1.
DR DIP; DIP-9123N; -.
DR IntAct; P08202; 4.
DR STRING; 511145.b0062; -.
DR jPOST; P08202; -.
DR PaxDb; P08202; -.
DR PRIDE; P08202; -.
DR DNASU; 947511; -.
DR EnsemblBacteria; AAC73173; AAC73173; b0062.
DR EnsemblBacteria; BAB96631; BAB96631; BAB96631.
DR GeneID; 947511; -.
DR KEGG; ecj:JW0061; -.
DR KEGG; eco:b0062; -.
DR PATRIC; fig|1411691.4.peg.2221; -.
DR EchoBASE; EB0050; -.
DR eggNOG; COG2160; Bacteria.
DR HOGENOM; CLU_045663_0_0_6; -.
DR InParanoid; P08202; -.
DR OMA; HMLEICP; -.
DR PhylomeDB; P08202; -.
DR BioCyc; EcoCyc:ARABISOM-MON; -.
DR BioCyc; MetaCyc:ARABISOM-MON; -.
DR BRENDA; 5.3.1.4; 2026.
DR UniPathway; UPA00145; UER00565.
DR EvolutionaryTrace; P08202; -.
DR PRO; PR:P08202; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008733; F:L-arabinose isomerase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019568; P:arabinose catabolic process; IMP:EcoliWiki.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IMP:EcoCyc.
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 SUPFAM; SSF50443; SSF50443; 1.
DR SUPFAM; SSF53743; SSF53743; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arabinose catabolism; Carbohydrate metabolism; Isomerase;
KW Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..500
FT /note="L-arabinose isomerase"
FT /id="PRO_0000198385"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 450
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT CONFLICT 72
FT /note="R -> P (in Ref. 1; AAA23463)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="K -> E (in Ref. 1; AAA23463)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> V (in Ref. 1; AAA23463)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 23..41
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2AJT"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 154..173
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 250..270
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:4F2D"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:4F2D"
FT TURN 372..375
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 389..398
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 400..412
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 435..444
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 459..468
FT /evidence="ECO:0007829|PDB:4F2D"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:4F2D"
FT HELIX 482..496
FT /evidence="ECO:0007829|PDB:4F2D"
SQ SEQUENCE 500 AA; 56074 MW; E427A145A3455D36 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
PATQIHGKKR 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
