ARAA_ALKHC
ID ARAA_ALKHC Reviewed; 497 AA.
AC Q9KBQ2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=L-arabinose isomerase {ECO:0000255|HAMAP-Rule:MF_00519};
DE EC=5.3.1.4 {ECO:0000255|HAMAP-Rule:MF_00519};
GN Name=araA {ECO:0000255|HAMAP-Rule:MF_00519}; OrderedLocusNames=BH1873;
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 conversion of L-arabinose to L-ribulose.
CC {ECO:0000255|HAMAP-Rule:MF_00519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-L-arabinopyranose = L-ribulose; Xref=Rhea:RHEA:14821,
CC ChEBI:CHEBI:16880, ChEBI:CHEBI:40886; EC=5.3.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00519};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00519};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00519};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 1/3. {ECO:0000255|HAMAP-Rule:MF_00519}.
CC -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00519}.
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DR EMBL; BA000004; BAB05592.1; -; Genomic_DNA.
DR PIR; A83884; A83884.
DR RefSeq; WP_010898034.1; NC_002570.2.
DR AlphaFoldDB; Q9KBQ2; -.
DR SMR; Q9KBQ2; -.
DR STRING; 272558.10174491; -.
DR EnsemblBacteria; BAB05592; BAB05592; BAB05592.
DR KEGG; bha:BH1873; -.
DR eggNOG; COG2160; Bacteria.
DR HOGENOM; CLU_045663_0_0_9; -.
DR OMA; HMLEICP; -.
DR OrthoDB; 507566at2; -.
DR BRENDA; 5.3.1.4; 661.
DR SABIO-RK; Q9KBQ2; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008733; F:L-arabinose isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10940; -; 1.
DR HAMAP; MF_00519; Arabinose_Isome; 1.
DR InterPro; IPR024664; Ara_Isoase_C.
DR InterPro; IPR038583; AraA_N_sf.
DR InterPro; IPR004216; Fuc/Ara_isomerase_C.
DR InterPro; IPR009015; Fucose_isomerase_N/cen_sf.
DR InterPro; IPR003762; Lara_isomerase.
DR PANTHER; PTHR38464; PTHR38464; 1.
DR Pfam; PF11762; Arabinose_Iso_C; 1.
DR Pfam; PF02610; Arabinose_Isome; 1.
DR PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR SUPFAM; SSF50443; SSF50443; 1.
DR SUPFAM; SSF53743; SSF53743; 1.
PE 3: Inferred from homology;
KW Arabinose catabolism; Carbohydrate metabolism; Isomerase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..497
FT /note="L-arabinose isomerase"
FT /id="PRO_0000198379"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 447
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ SEQUENCE 497 AA; 56320 MW; 637D660D25E3F5A4 CRC64;
MLQTKPYTFW FITGSQHLYG EDAIEQVRQH SQTMVEKLNK IGELPYTIEL KEVLTTPDAI
RKMVIAANSD DDCAGMITWM HTFSPAKMWI NGLKQLKKPL LHLHTQFNRE IPYDDIDMDF
MNLNQSAHGD REYGHIGARL NISRKVIVGH WQNNDVQERL GAWMRTAAAF VDGHHLKVAR
FGDNMREVAV TEGDKVEAQI QFGWSITAFG IGDLVEKMKA VSEDEVRRLF DEYQELYRLS
PSILEQDEVK AAVLEQAKME LALKEFLEEG GYTAFTTNFE DLHGMKQLPG LAVQRLMAEG
YGFGGEGDWK TAALLRMMKI IADGKGTSFM EDYTYHLAEG NELVLGSHML EICPTIAANQ
PEIQVHPLGI GGKEDPARLV FDGADGPALN ASLIDLGHRF RLVVNEVEAI KPERDMPKLP
VAKVLWKCKP SLSEATEAWI HAGGAHHTVF SFEVTPEQLY DWATLADIEV VFINDKTDVL
QFQQQLQWNE AFRRLFK
