ID   RHAA_RHOBA              Reviewed;         427 AA.
AC   Q7UYE5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=L-rhamnose isomerase {ECO:0000255|HAMAP-Rule:MF_00541};
DE            EC=5.3.1.14 {ECO:0000255|HAMAP-Rule:MF_00541};
GN   Name=rhaA {ECO:0000255|HAMAP-Rule:MF_00541}; OrderedLocusNames=RB678;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC   -!- FUNCTION: Catalyzes the interconversion of L-rhamnose and L-rhamnulose.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00541};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00541};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00541};
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC       phosphate from L-rhamnose: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00541}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00541}.
CC   -!- SIMILARITY: Belongs to the rhamnose isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00541, ECO:0000305}.
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DR   EMBL; BX294134; CAD71697.1; -; Genomic_DNA.
DR   RefSeq; NP_864023.1; NC_005027.1.
DR   RefSeq; WP_011118020.1; NC_005027.1.
DR   AlphaFoldDB; Q7UYE5; -.
DR   SMR; Q7UYE5; -.
DR   STRING; 243090.RB678; -.
DR   EnsemblBacteria; CAD71697; CAD71697; RB678.
DR   KEGG; rba:RB678; -.
DR   PATRIC; fig|243090.15.peg.326; -.
DR   eggNOG; COG4806; Bacteria.
DR   HOGENOM; CLU_052790_0_0_0; -.
DR   InParanoid; Q7UYE5; -.
DR   OMA; HKVNLHA; -.
DR   OrthoDB; 283831at2; -.
DR   UniPathway; UPA00541; UER00601.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008740; F:L-rhamnose isomerase activity; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019324; P:L-lyxose metabolic process; IBA:GO_Central.
DR   GO; GO:0019301; P:rhamnose catabolic process; IBA:GO_Central.
DR   HAMAP; MF_00541; RhaA; 1.
DR   InterPro; IPR009308; Rhamnose_isomerase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   Pfam; PF06134; RhaA; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR01748; rhaA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Manganese; Metal-binding; Reference proteome;
KW   Rhamnose metabolism.
FT   CHAIN           1..427
FT                   /note="L-rhamnose isomerase"
FT                   /id="PRO_0000090563"
FT   BINDING         264
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT   BINDING         298
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
SQ   SEQUENCE   427 AA;  47748 MW;  32F8BCF9513452DA CRC64;
     MNRAGNIEKA FELAREEYQA IGVDVDSALQ RMRDVEISVH CWQGDDVKGF EGDDGALGNG
     LAVTGNYPGR ARTIDELQSD LELAYSLIPG NHRLNLHALY GEFKGRVDRD EIEVEHFQGW
     IDWARDQKVR LDFNPSYFSH PNAADGFTLA HADSGIRQFW IDHGIACRKI AAAMGAAQSN
     PCINNFWVPD GYKDVPADRK APRERLADSL DSIFATEYPA EQTLDAVECK LFGIGSESYV
     VGSHEFYMGY AMSRYKVLCL DAGHFHPTET ISDKISAVMM YVPELLLHVS RGVRWDSDHV
     VTYSDELQSI MQEVVRGDYL GRVHIGLDFF DASINRVAAW AIGTRNALKA VLAALLEPTE
     QLRKMELEGD LTGRLALLEE QKTLPLGAVW NHYCQSVDVP AGSDWLENVR QYESQVLSQR
     SDSSALV