RHAM_SHIF8
ID RHAM_SHIF8 Reviewed; 104 AA.
AC Q0SZ91;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=L-rhamnose mutarotase {ECO:0000255|HAMAP-Rule:MF_01663};
DE EC=5.1.3.32 {ECO:0000255|HAMAP-Rule:MF_01663};
DE AltName: Full=Rhamnose 1-epimerase {ECO:0000255|HAMAP-Rule:MF_01663};
DE AltName: Full=Type-3 mutarotase {ECO:0000255|HAMAP-Rule:MF_01663};
GN Name=rhaM {ECO:0000255|HAMAP-Rule:MF_01663}; OrderedLocusNames=SFV_3594;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
CC -!- FUNCTION: Involved in the anomeric conversion of L-rhamnose.
CC {ECO:0000255|HAMAP-Rule:MF_01663}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-rhamnose = beta-L-rhamnose; Xref=Rhea:RHEA:25584,
CC ChEBI:CHEBI:27586, ChEBI:CHEBI:27907; EC=5.1.3.32;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01663};
CC -!- PATHWAY: Carbohydrate metabolism; L-rhamnose metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01663}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01663}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01663}.
CC -!- SIMILARITY: Belongs to the rhamnose mutarotase family.
CC {ECO:0000255|HAMAP-Rule:MF_01663}.
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; CP000266; ABF05624.1; -; Genomic_DNA.
DR RefSeq; WP_000619511.1; NC_008258.1.
DR AlphaFoldDB; Q0SZ91; -.
DR SMR; Q0SZ91; -.
DR EnsemblBacteria; ABF05624; ABF05624; SFV_3594.
DR GeneID; 58391207; -.
DR KEGG; sfv:SFV_3594; -.
DR HOGENOM; CLU_100689_2_0_6; -.
DR OMA; KRHDEIW; -.
DR BioCyc; SFLE373384:SFV_RS19815-MON; -.
DR UniPathway; UPA00125; -.
DR Proteomes; UP000000659; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0062192; F:L-rhamnose mutarotase activity; IEA:UniProtKB-EC.
DR GO; GO:0019299; P:rhamnose metabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01663; L_rham_rotase; 1.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR013448; L-rhamnose_mutarotase.
DR InterPro; IPR008000; Rham/fucose_mutarotase.
DR Pfam; PF05336; rhaM; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR02625; YiiL_rotase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Rhamnose metabolism.
FT CHAIN 1..104
FT /note="L-rhamnose mutarotase"
FT /id="PRO_0000344607"
FT ACT_SITE 22
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
FT BINDING 76..77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01663"
SQ SEQUENCE 104 AA; 12293 MW; 6A277307F0F1C8F2 CRC64;
MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGVHN YAIYLDKARN LLFAMVEIES
EERWNAVAST DVCQRWWKYM TDVMPANPDN SPVSSELQEV FYLP
