ID RHAM_AGRT5 Reviewed; 107 AA. AC A9CFA8; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 24-NOV-2009, entry version 13. DE RecName: Full=L-rhamnose mutarotase; DE EC=5.1.3.n3; DE AltName: Full=Rhamnose 1-epimerase; DE AltName: Full=Type-3 mutarotase; GN Name=rhaM; OrderedLocusNames=Atu3491; ORFNames=AGR_L_2674; OS Agrobacterium tumefaciens (strain C58 / ATCC 33970). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21608551; PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., RA Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21608550; PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., RA Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). CC -!- FUNCTION: Involved in the anomeric conversion of L-rhamnose (By CC similarity). CC -!- CATALYTIC ACTIVITY: Alpha-L-rhamnose = beta-L-rhamnose. CC -!- PATHWAY: Carbohydrate metabolism; L-rhamnose metabolism. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the rhamnose mutarotase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE007870; AAK89903.1; -; Genomic_DNA. DR PIR; AB2986; AB2986. DR PIR; E98297; E98297. DR RefSeq; NP_357118.1; -. DR STRING; A9CFA8; -. DR GeneID; 1135365; -. DR GenomeReviews; AE007870_GR; Atu3491. DR KEGG; atu:Atu3491; -. DR OMA; VMKKWWA; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016857; F:racemase and epimerase activity, acting on ...; IEA:EC. DR GO; GO:0019299; P:rhamnose metabolic process; IEA:HAMAP. DR HAMAP; MF_01663; -; 1. DR InterPro; IPR013448; L-rhamnose_1-epimerase. DR InterPro; IPR008000; Rhamnose_mutarotase. DR Pfam; PF05336; DUF718; 1. DR TIGRFAMs; TIGR02625; YiiL_rotase; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Rhamnose metabolism. FT CHAIN 1 107 L-rhamnose mutarotase. FT /FTId=PRO_0000344550. FT REGION 79 80 Substrate binding (By similarity). FT ACT_SITE 25 25 Proton donor (By similarity). FT BINDING 21 21 Substrate (By similarity). FT BINDING 44 44 Substrate (By similarity). SQ SEQUENCE 107 AA; 12278 MW; D8288A26D8EE50B7 CRC64; MPELEKHAFR MKLFAGKEVE YKKRHDEIWP ELVALLHEAG VSDYSIHLDP ETSILFGVLT RPKVHGMAAL PEHPVMKKWW AHMADIMESN PDNSPVAKDL VTVFHLP //