RHAA_ECOLI
ID RHAA_ECOLI Reviewed; 419 AA.
AC P32170; Q2M8K0; Q6BEY0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=L-rhamnose isomerase {ECO:0000255|HAMAP-Rule:MF_00541, ECO:0000303|PubMed:14243758};
DE Short=RhamIso {ECO:0000303|PubMed:8564401};
DE EC=5.3.1.14 {ECO:0000255|HAMAP-Rule:MF_00541, ECO:0000269|PubMed:14243758, ECO:0000269|PubMed:1650346, ECO:0000269|PubMed:8564401};
GN Name=rhaA {ECO:0000255|HAMAP-Rule:MF_00541};
GN OrderedLocusNames=b3903, JW5561;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8396120; DOI=10.1128/jb.175.17.5585-5594.1993;
RA Moralejo P., Egan S.M., Hidalgo E.F., Aguilar J.;
RT "Sequencing and characterization of a gene cluster encoding the enzymes for
RT L-rhamnose metabolism in Escherichia coli.";
RL J. Bacteriol. 175:5585-5594(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 SEQUENCE REVISION TO 359-360.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=B;
RX PubMed=14243758; DOI=10.1016/0926-6569(64)90263-9;
RA Takagi Y., Sawada H.;
RT "The metabolism of L-rhamnose in Escherichia coli. I. L-rhamnose
RT isomerase.";
RL Biochim. Biophys. Acta 92:10-17(1964).
RN [7]
RP FUNCTION.
RX PubMed=2558952; DOI=10.1016/0378-1097(89)90226-7;
RA Badia J., Baldoma L., Aguilar J., Boronat A.;
RT "Identification of the rhaA, rhaB and rhaD gene products from Escherichia
RT coli K-12.";
RL FEMS Microbiol. Lett. 65:253-257(1989).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1650346; DOI=10.1128/jb.173.16.5144-5150.1991;
RA Badia J., Gimenez R., Baldoma L., Barnes E., Fessner W.D., Aguilar J.;
RT "L-lyxose metabolism employs the L-rhamnose pathway in mutant cells of
RT Escherichia coli adapted to grow on L-lyxose.";
RL J. Bacteriol. 173:5144-5150(1991).
RN [9]
RP INDUCTION.
RC STRAIN=ECL116;
RX PubMed=8230210; DOI=10.1006/jmbi.1993.1565;
RA Egan S.M., Schleif R.F.;
RT "A regulatory cascade in the induction of rhaBAD.";
RL J. Mol. Biol. 234:87-98(1993).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8564401; DOI=10.1016/0968-0896(95)00119-2;
RA Garcia-Junceda E., Shen G.J., Alajarin R., Wong C.H.;
RT "Cloning and overexpression of rhamnose isomerase and fucose isomerase.";
RL Bioorg. Med. Chem. 3:1349-1355(1995).
RN [11]
RP INDUCTION.
RX PubMed=10852886; DOI=10.1128/jb.182.12.3529-3535.2000;
RA Holcroft C.C., Egan S.M.;
RT "Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of
RT the alpha subunit in transcription activation of the Escherichia coli
RT rhaBAD operon.";
RL J. Bacteriol. 182:3529-3535(2000).
RN [12] {ECO:0007744|PDB:1D8W, ECO:0007744|PDB:1DE5, ECO:0007744|PDB:1DE6}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MANGANESE; ZINC AND
RP ALDEHYDO-L-RHAMNOSE, COFACTOR, AND SUBUNIT.
RX PubMed=10891278; DOI=10.1006/jmbi.2000.3896;
RA Korndoerfer I.P., Fessner W.-D., Matthews B.W.;
RT "The structure of rhamnose isomerase from Escherichia coli and its relation
RT with xylose isomerase illustrates a change between inter and intra-subunit
RT complementation during evolution.";
RL J. Mol. Biol. 300:917-933(2000).
CC -!- FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose
CC (PubMed:14243758, PubMed:2558952, PubMed:8564401, PubMed:1650346). Can
CC also catalyze the isomerization of L-lyxose to L-xylulose
CC (PubMed:1650346). {ECO:0000269|PubMed:14243758,
CC ECO:0000269|PubMed:1650346, ECO:0000269|PubMed:2558952,
CC ECO:0000269|PubMed:8564401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-rhamnopyranose = L-rhamnulose; Xref=Rhea:RHEA:23160,
CC ChEBI:CHEBI:17897, ChEBI:CHEBI:62346; EC=5.3.1.14;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00541,
CC ECO:0000269|PubMed:14243758, ECO:0000269|PubMed:1650346,
CC ECO:0000269|PubMed:8564401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lyxopyranose = L-xylulose; Xref=Rhea:RHEA:28058,
CC ChEBI:CHEBI:17399, ChEBI:CHEBI:62321;
CC Evidence={ECO:0000269|PubMed:1650346};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00541,
CC ECO:0000269|PubMed:10891278, ECO:0000269|PubMed:14243758};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00541,
CC ECO:0000269|PubMed:10891278};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 mM for L-rhamnose {ECO:0000269|PubMed:14243758,
CC ECO:0000269|PubMed:1650346};
CC KM=5 mM for L-lyxose {ECO:0000269|PubMed:1650346};
CC KM=1.7 mM for L-rhamnulose {ECO:0000269|PubMed:14243758};
CC Vmax=6.2 umol/min/mg enzyme with L-rhamnose as substrate
CC {ECO:0000269|PubMed:1650346};
CC Vmax=6.0 umol/min/mg enzyme with L-lyxose as substrate
CC {ECO:0000269|PubMed:1650346};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:14243758};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC phosphate from L-rhamnose: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00541,
CC ECO:0000305|PubMed:2558952}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00541,
CC ECO:0000269|PubMed:10891278}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00541,
CC ECO:0000305}.
CC -!- INDUCTION: Induced by L-rhamnose via the RhaR-RhaS regulatory cascade.
CC Binding of the cAMP receptor protein (CRP) is required for full
CC expression (PubMed:10852886, PubMed:8230210). Also induced by L-lyxose
CC (PubMed:1650346). {ECO:0000269|PubMed:10852886,
CC ECO:0000269|PubMed:1650346, ECO:0000269|PubMed:8230210}.
CC -!- MISCELLANEOUS: In the crystal structure, RhaA appears to bind a zinc
CC ion at a structural site. However, the metal ion may be different in
CC vivo.
CC -!- SIMILARITY: Belongs to the rhamnose isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00541, ECO:0000305}.
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DR EMBL; X60472; CAA43002.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03036.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48234.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77406.1; -; Genomic_DNA.
DR PIR; S40847; S40847.
DR RefSeq; WP_001311268.1; NZ_SSZK01000014.1.
DR RefSeq; YP_026276.1; NC_000913.3.
DR PDB; 1D8W; X-ray; 1.60 A; A/B/C/D=1-419.
DR PDB; 1DE5; X-ray; 2.20 A; A/B/C/D=1-419.
DR PDB; 1DE6; X-ray; 2.10 A; A/B/C/D=1-419.
DR PDBsum; 1D8W; -.
DR PDBsum; 1DE5; -.
DR PDBsum; 1DE6; -.
DR AlphaFoldDB; P32170; -.
DR SMR; P32170; -.
DR DIP; DIP-10690N; -.
DR STRING; 511145.b3903; -.
DR DrugBank; DB02399; L-Rhamnitol.
DR DrugBank; DB02961; Rhamnose.
DR PaxDb; P32170; -.
DR PRIDE; P32170; -.
DR EnsemblBacteria; AAT48234; AAT48234; b3903.
DR EnsemblBacteria; BAE77406; BAE77406; BAE77406.
DR GeneID; 948400; -.
DR KEGG; ecj:JW5561; -.
DR KEGG; eco:b3903; -.
DR PATRIC; fig|1411691.4.peg.2803; -.
DR EchoBASE; EB1813; -.
DR eggNOG; COG4806; Bacteria.
DR HOGENOM; CLU_052790_0_0_6; -.
DR InParanoid; P32170; -.
DR OMA; HKVNLHA; -.
DR PhylomeDB; P32170; -.
DR BioCyc; EcoCyc:RHAMNISOM-MON; -.
DR BioCyc; MetaCyc:RHAMNISOM-MON; -.
DR BRENDA; 5.3.1.14; 2026.
DR UniPathway; UPA00541; UER00601.
DR EvolutionaryTrace; P32170; -.
DR PRO; PR:P32170; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0008740; F:L-rhamnose isomerase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:CAFA.
DR GO; GO:0033296; F:rhamnose binding; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0019324; P:L-lyxose metabolic process; IEP:EcoCyc.
DR GO; GO:0019301; P:rhamnose catabolic process; IMP:EcoCyc.
DR DisProt; DP00429; -.
DR HAMAP; MF_00541; RhaA; 1.
DR InterPro; IPR009308; Rhamnose_isomerase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR Pfam; PF06134; RhaA; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR01748; rhaA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Manganese; Metal-binding;
KW Reference proteome; Rhamnose metabolism; Zinc.
FT CHAIN 1..419
FT /note="L-rhamnose isomerase"
FT /id="PRO_0000090552"
FT BINDING 95
FT /ligand="L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:16055"
FT /evidence="ECO:0000269|PubMed:10891278,
FT ECO:0007744|PDB:1DE6"
FT BINDING 226..228
FT /ligand="L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:16055"
FT /evidence="ECO:0000269|PubMed:10891278,
FT ECO:0007744|PDB:1DE6"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:10891278,
FT ECO:0007744|PDB:1D8W, ECO:0007744|PDB:1DE5,
FT ECO:0007744|PDB:1DE6"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:10891278,
FT ECO:0007744|PDB:1D8W, ECO:0007744|PDB:1DE5,
FT ECO:0007744|PDB:1DE6"
FT BINDING 262
FT /ligand="L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:16055"
FT /evidence="ECO:0000269|PubMed:10891278,
FT ECO:0007744|PDB:1DE6"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541,
FT ECO:0000269|PubMed:10891278, ECO:0007744|PDB:1DE6"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:10891278,
FT ECO:0007744|PDB:1D8W, ECO:0007744|PDB:1DE5,
FT ECO:0007744|PDB:1DE6"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541,
FT ECO:0000269|PubMed:10891278, ECO:0007744|PDB:1DE6"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541,
FT ECO:0000269|PubMed:10891278, ECO:0007744|PDB:1DE6"
FT BINDING 326
FT /ligand="L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:16055"
FT /evidence="ECO:0000269|PubMed:10891278,
FT ECO:0007744|PDB:1DE6"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:10891278,
FT ECO:0007744|PDB:1D8W, ECO:0007744|PDB:1DE5,
FT ECO:0007744|PDB:1DE6"
FT CONFLICT 359..360
FT /note="EL -> DV (in Ref. 2; AAB03036)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="A -> P (in Ref. 1; CAA43002)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1D8W"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1DE6"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 152..176
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:1D8W"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:1D8W"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:1D8W"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:1D8W"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 334..353
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:1D8W"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:1D8W"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:1D8W"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:1D8W"
SQ SEQUENCE 419 AA; 47199 MW; D237E95BD24999BA CRC64;
MTTQLEQAWE LAKQRFAAVG IDVEEALRQL DRLPVSMHCW QGDDVSGFEN PEGSLTGGIQ
ATGNYPGKAR NASELRADLE QAMRLIPGPK RLNLHAIYLE SDTPVSRDQI KPEHFKNWVE
WAKANQLGLD FNPSCFSHPL SADGFTLSHA DDSIRQFWID HCKASRRVSA YFGEQLGTPS
VMNIWIPDGM KDITVDRLAP RQRLLAALDE VISEKLNPAH HIDAVESKLF GIGAESYTVG
SNEFYMGYAT SRQTALCLDA GHFHPTEVIS DKISAAMLYV PQLLLHVSRP VRWDSDHVVL
LDDETQAIAS EIVRHDLFDR VHIGLDFFDA SINRIAAWVI GTRNMKKALL RALLEPTAEL
RKLEAAGDYT ARLALLEEQK SLPWQAVWEM YCQRHDTPAG SEWLESVRAY EKEILSRRG
