PLH21_FORAG
ID PLH21_FORAG Reviewed; 104 AA.
AC T2KM13;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=L-rhamnose mutarotase {ECO:0000303|PubMed:31285597};
DE EC=5.1.3.32 {ECO:0000269|PubMed:31285597};
DE AltName: Full=P21_mutarotase {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P21 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P21;
DE AltName: Full=Rhamnose 1-epimerase;
DE AltName: Full=Type-3 mutarotase;
GN Name=rhaM; ORFNames=BN863_22100;
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX PubMed=23995932; DOI=10.1128/aem.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA Bornscheuer U.T., Hehemann J.H.;
RT "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT ulvan.";
RL Nat. Chem. Biol. 15:803-812(2019).
CC -!- FUNCTION: L-rhamnose mutarotase involved in ulvan degradation
CC (PubMed:31285597). Ulvan is the main polysaccharide component of the
CC Ulvales (green seaweed) cell wall. It is composed of disaccharide
CC building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-
CC glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl)
CC (Probable). L-rhamnose mutarotase catalyzes the anomeric conversion of
CC alpha- to beta-L-rhamnose (PubMed:31285597).
CC {ECO:0000269|PubMed:31285597, ECO:0000305|PubMed:31285597}.
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:0000269|PubMed:31285597};
CC -!- PATHWAY: Carbohydrate metabolism; L-rhamnose metabolism.
CC {ECO:0000250|UniProtKB:P32156}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31285597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the rhamnose mutarotase family. {ECO:0000305}.
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DR EMBL; HG315671; CDF79922.1; -; Genomic_DNA.
DR RefSeq; WP_038530514.1; NZ_HG315671.1.
DR PDB; 6HHN; X-ray; 1.47 A; A=2-104.
DR PDBsum; 6HHN; -.
DR AlphaFoldDB; T2KM13; -.
DR SMR; T2KM13; -.
DR STRING; 1347342.BN863_22100; -.
DR EnsemblBacteria; CDF79922; CDF79922; BN863_22100.
DR PATRIC; fig|1347342.6.peg.2217; -.
DR eggNOG; COG3254; Bacteria.
DR HOGENOM; CLU_100689_2_0_10; -.
DR OMA; KRHDEIW; -.
DR OrthoDB; 1694303at2; -.
DR UniPathway; UPA00125; -.
DR Proteomes; UP000016160; 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-UniPathway.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase;
KW Reference proteome; Rhamnose metabolism.
FT CHAIN 1..104
FT /note="L-rhamnose mutarotase"
FT /id="PRO_0000448333"
FT ACT_SITE 22
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q7BSH1"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7BSH1"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7BSH1"
FT BINDING 76..77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7BSH1"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:6HHN"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:6HHN"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:6HHN"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:6HHN"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6HHN"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:6HHN"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6HHN"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:6HHN"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:6HHN"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6HHN"
SQ SEQUENCE 104 AA; 12199 MW; 81B9745B95805C76 CRC64;
MERLAFKMKL NKGQKQAYKE RHDQLWPELK QLLKDNGVSE YSIFIDEETN TLFAFQKVSG
HGGSQDLANN EIVKKWWDFM ADIMQVNPDN SPVSIPLEEV FYME
