ARAA_SHIDS
ID ARAA_SHIDS Reviewed; 500 AA.
AC Q32K31;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=SDY_0089;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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 -!- SUBUNIT: Homohexamer. {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; CP000034; ABB60326.1; -; Genomic_DNA.
DR RefSeq; WP_000151756.1; NC_007606.1.
DR RefSeq; YP_401815.1; NC_007606.1.
DR AlphaFoldDB; Q32K31; -.
DR SMR; Q32K31; -.
DR STRING; 300267.SDY_0089; -.
DR EnsemblBacteria; ABB60326; ABB60326; SDY_0089.
DR KEGG; sdy:SDY_0089; -.
DR PATRIC; fig|300267.13.peg.104; -.
DR HOGENOM; CLU_045663_0_0_6; -.
DR OMA; HMLEICP; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000002716; 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..500
FT /note="L-arabinose isomerase"
FT /id="PRO_0000259344"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 450
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ SEQUENCE 500 AA; 56105 MW; 18077C85A9335FDA CRC64;
MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTTPDEI
TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF
MNLNQTAHGG REFSFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR
FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT
PATQIHGEKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAA
EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP
KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT
RLPAFKDALR WNEVYYGFRR