RHAA_ALKHC
ID RHAA_ALKHC Reviewed; 418 AA.
AC Q9KCL9;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=BH1552;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05271.1; -; Genomic_DNA.
DR PIR; H83843; H83843.
DR RefSeq; WP_010897715.1; NC_002570.2.
DR PDB; 3P14; X-ray; 2.51 A; A/B/C/D=1-418.
DR PDB; 3UU0; X-ray; 2.70 A; A/B/C/D=1-418.
DR PDB; 3UVA; X-ray; 2.69 A; A/B/C/D=1-418.
DR PDB; 3UXI; X-ray; 2.73 A; A/B/C/D=1-418.
DR PDBsum; 3P14; -.
DR PDBsum; 3UU0; -.
DR PDBsum; 3UVA; -.
DR PDBsum; 3UXI; -.
DR AlphaFoldDB; Q9KCL9; -.
DR SMR; Q9KCL9; -.
DR MINT; Q9KCL9; -.
DR STRING; 272558.10174169; -.
DR EnsemblBacteria; BAB05271; BAB05271; BAB05271.
DR KEGG; bha:BH1552; -.
DR eggNOG; COG4806; Bacteria.
DR HOGENOM; CLU_052790_0_0_9; -.
DR OMA; HKVNLHA; -.
DR OrthoDB; 283831at2; -.
DR UniPathway; UPA00541; UER00601.
DR EvolutionaryTrace; Q9KCL9; -.
DR Proteomes; UP000001258; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Manganese; Metal-binding;
KW Reference proteome; Rhamnose metabolism.
FT CHAIN 1..418
FT /note="L-rhamnose isomerase"
FT /id="PRO_0000090549"
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"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:3P14"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3P14"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3UU0"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3UVA"
FT HELIX 151..175
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:3P14"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3P14"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:3P14"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:3P14"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3UVA"
FT HELIX 333..352
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 368..377
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:3P14"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:3P14"
FT HELIX 402..412
FT /evidence="ECO:0007829|PDB:3P14"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:3P14"
SQ SEQUENCE 418 AA; 48178 MW; 10165258A259864F CRC64;
MSMKSQFERA KIEYGQWGID VEEALERLKQ VPISIHCWQG DDVGGFELSK GELSGGIDVT
GDYPGKATTP EELRMDLEKA LSLIPGKHRV NLHAIYAETD GKVVERDQLE PRHFEKWVRW
AKRHGLGLDF NPTLFSHEKA KDGLTLAHPD QAIRQFWIDH CIASRKIGEY FGKELETPCL
TNIWIPDGYK DTPSDRLTPR KRLKESLDQI FAAEINEAYN LDAVESKLFG IGSESYVVGS
HEFYLSYALK NDKLCLLDTG HYHPTETVSN KISAMLLFHD KLALHVSRPV RWDSDHVVTF
DDELREIALE IVRNDALDRV LIGLDFFDAS INRIAAWTIG TRNVIKALLF AMLIPHKQLK
EWQETGDYTR RLAVLEEFKT YPLGAIWNEY CERMNVPIKE EWLKEIAIYE KEVLLQRH
