RHAA_CLOB8
ID RHAA_CLOB8 Reviewed; 418 AA.
AC A6LQK4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Cbei_0446;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000721; ABR32634.1; -; Genomic_DNA.
DR RefSeq; WP_011967795.1; NC_009617.1.
DR AlphaFoldDB; A6LQK4; -.
DR SMR; A6LQK4; -.
DR STRING; 290402.Cbei_0446; -.
DR EnsemblBacteria; ABR32634; ABR32634; Cbei_0446.
DR KEGG; cbe:Cbei_0446; -.
DR eggNOG; COG4806; Bacteria.
DR HOGENOM; CLU_052790_0_0_9; -.
DR OMA; HKVNLHA; -.
DR OrthoDB; 283831at2; -.
DR UniPathway; UPA00541; UER00601.
DR Proteomes; UP000000565; Chromosome.
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:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
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; Rhamnose metabolism.
FT CHAIN 1..418
FT /note="L-rhamnose isomerase"
FT /id="PRO_1000081935"
FT BINDING 261
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
FT BINDING 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00541"
SQ SEQUENCE 418 AA; 48128 MW; 560ED6C61A7DEF9E CRC64;
MNVKEKYELA KKEYEKWGID VDKVLDELNK VKISIHCWQG DDVKGFEVVQ NELSGGIQCN
GNYPGAARNA EELRKDLDKA LSLIPGKHKV NLHAIYLETN GEFVDRDEIK PEHFANWVKW
AKENGLGLDF NPTIFSHPKS ADGLTLSHPD KEIRDFWIRH SIASRKIGEY FGKELGQTCL
TNIWIPDGYK DIPSDRLGPR RRLKESLDEI FKVQIDKKYN LDCVESKVFG IGAEAYTVGS
NEFYLNYAAK NNIMSLMDTG HYHPTEVVSD KLSAMLLFDE KVALHVSRPV RWDSDHVVVY
DDELKEIAKE IVRNDALDRV IIGLDFFDAS INRIAAWTIG SRNMIKALLN AMLTPNDKLR
ELQEEGNFTE RLALMEEFKT YPMGDIWNYY CEKNNVPVGE SWIKEVKEYE KDVLSKRN