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Entry: A0A3A9KBB6_9BACI
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ID   A0A3A9KBB6_9BACI        Unreviewed;       418 AA.
AC   A0A3A9KBB6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   18-JUN-2025, entry version 22.
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:RKL66863.1};
GN   ORFNames=CR203_13615 {ECO:0000313|EMBL:RKL66863.1};
OS   Salipaludibacillus neizhouensis.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=885475 {ECO:0000313|EMBL:RKL66863.1, ECO:0000313|Proteomes:UP000281498};
RN   [1] {ECO:0000313|EMBL:RKL66863.1, ECO:0000313|Proteomes:UP000281498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13187 {ECO:0000313|EMBL:RKL66863.1,
RC   ECO:0000313|Proteomes:UP000281498};
RA   Wang H.;
RT   "Bacillus sp. nov., a halophilic bacterium isolated from a Keqin Lake.";
RL   Submitted (OCT-2017) 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:RKL66863.1}.
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DR   EMBL; PDOE01000005; RKL66863.1; -; Genomic_DNA.
DR   RefSeq; WP_110934718.1; NZ_KZ614146.1.
DR   AlphaFoldDB; A0A3A9KBB6; -.
DR   OrthoDB; 9766697at2; -.
DR   UniPathway; UPA00541; UER00601.
DR   Proteomes; UP000281498; 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:UP000281498};
KW   Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW   Rule:MF_00541}.
FT   BINDING         261
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00541"
FT   BINDING         293
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00541"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00541"
SQ   SEQUENCE   418 AA;  48089 MW;  ADFCD27E0202DA34 CRC64;
     MTVKENFELA KKAYEKWDID IDHVFAQLKQ VPISIHCWQG DDIGGFEVNQ SELSGGIEVT
     GDYPGKATTP EELRQDIEKA LSLIPGKHRI NLHAIYAETD GIAVERDELE PKHFEKWVQW
     AKKNGLGLDF NPTLFSHEKA SSGLTLSHPD KEIRQFWIDH CIASRKIGEY FGKELGTPCL
     TNIWIPDGYK DTPSDRLTPR RRLKESLDEI YTVKLDEKFN IDAVESKVFG IGSESYVVGS
     HEFYYGYALK NDKLCLLDTG HYHPTEMVSN KISSMLLYSE KLALHVSRPV RWDSDHVVTL
     DDELKELALE IVRNDALNRV IIGLDFFDAS INRVAAWTIG TRNMIKALML GMLMPNEHLK
     QLQEDGNFTE RLALLEEFKT YPFGAIWDYY CETMGVPERE NWLNDVKQYE KEVLSHRE
//
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