RHAM_SALG2
ID RHAM_SALG2 Reviewed; 104 AA.
AC B5RFC8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=SG3379;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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}.
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DR EMBL; AM933173; CAR39171.1; -; Genomic_DNA.
DR RefSeq; WP_000619478.1; NC_011274.1.
DR AlphaFoldDB; B5RFC8; -.
DR SMR; B5RFC8; -.
DR EnsemblBacteria; CAR39171; CAR39171; SG3379.
DR KEGG; seg:SG3379; -.
DR HOGENOM; CLU_100689_2_0_6; -.
DR OMA; KRHDEIW; -.
DR UniPathway; UPA00125; -.
DR Proteomes; UP000008321; 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_1000187228"
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; 12334 MW; CBF4810E83A5C217 CRC64;
MIRKAFVMQV NADAHEEYQR RHNPIWPELE AVLKSHGAHH YAIYLDQERN LLFATVEIES
EERWNAVAST DVCQRWWKHM RDVMPANPDN SPVSAELKEV FYLQ