ID A0A917C675_9BACL Unreviewed; 418 AA.
AC A0A917C675;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE RecName: Full=L-rhamnose isomerase {ECO:0000256|HAMAP-Rule:MF_00541, ECO:0000256|NCBIfam:TIGR01748};
DE EC=5.3.1.14 {ECO:0000256|HAMAP-Rule:MF_00541, ECO:0000256|NCBIfam:TIGR01748};
GN Name=rhaA {ECO:0000256|HAMAP-Rule:MF_00541,
GN ECO:0000313|EMBL:GGF71001.1};
GN ORFNames=GCM10010912_15210 {ECO:0000313|EMBL:GGF71001.1};
OS Paenibacillus albidus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=2041023 {ECO:0000313|EMBL:GGF71001.1, ECO:0000313|Proteomes:UP000637643};
RN [1] {ECO:0000313|EMBL:GGF71001.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.16134 {ECO:0000313|EMBL:GGF71001.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:GGF71001.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.16134 {ECO:0000313|EMBL:GGF71001.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose.
CC {ECO:0000256|HAMAP-Rule:MF_00541}.
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:0000256|HAMAP-Rule:MF_00541};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00541};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00541};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC phosphate from L-rhamnose: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00541}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00541}.
CC -!- SIMILARITY: Belongs to the rhamnose isomerase family.
CC {ECO:0000256|HAMAP-Rule:MF_00541}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GGF71001.1}.
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DR EMBL; BMKR01000005; GGF71001.1; -; Genomic_DNA.
DR RefSeq; WP_189023512.1; NZ_BMKR01000005.1.
DR Proteomes; UP000637643; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008740; F:L-rhamnose isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019324; P:L-lyxose metabolic process; IEA:TreeGrafter.
DR GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR HAMAP; MF_00541; RhaA; 1.
DR InterPro; IPR050337; L-rhamnose_isomerase.
DR InterPro; IPR009308; Rhamnose_isomerase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR NCBIfam; NF002203; PRK01076.1; 1.
DR NCBIfam; TIGR01748; rhaA; 1.
DR PANTHER; PTHR30268; L-RHAMNOSE ISOMERASE; 1.
DR PANTHER; PTHR30268:SF0; L-RHAMNOSE ISOMERASE; 1.
DR Pfam; PF06134; RhaA; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00541};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00541};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00541};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00541}; Reference proteome {ECO:0000313|Proteomes:UP000637643};
KW Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW Rule:MF_00541}.
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00541"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00541"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00541"
SQ SEQUENCE 418 AA; 47658 MW; F23C75C25B971345 CRC64;
MEQSILNSYN EAKRLYALHG IDVEQVLEQL AEIKISLHCW QGDDVKGFLN KDKELGGGIA
VTGSYPGRAG TPEELRRDLE QALALIPGRH KVNLHAIYAD TEEEVELDKL EPKHFENWVH
WAKEQGLGLD FNPTCFSHEK AKDGFTLSHP DKEIRDFWIK HCQASRRIAE SFGQALGQPC
VTNFWVPDGY KDTPVDRLSP RVRLKESLDE IFSEKIDESY NIDAVESKLF GIGSESYVVG
SHEFYMGYAL SMGKAVCFDA GHFHPTEVIS NKLSSWLMFG DRLLLHVSRP VRWDSDHVVT
MDDELLEIAR ELVRGQLLDR THIGLDFFDG SINHIAAWVI GTRNTIKALL RAMLEPVETL
KQIELSGDYT SRLALVEEFK SYPFGAVWDY YCAKQGVPVR EGWLSEVKKY EQEVLLKR
//
