ID K0IGW6_9BACL Unreviewed; 494 AA.
AC K0IGW6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=L-arabinose isomerase {ECO:0000256|HAMAP-Rule:MF_00519};
DE EC=5.3.1.4 {ECO:0000256|HAMAP-Rule:MF_00519};
GN Name=araA {ECO:0000256|HAMAP-Rule:MF_00519,
GN ECO:0000313|EMBL:AFU48611.1};
OS Alicyclobacillus sp. TP7.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1202714 {ECO:0000313|EMBL:AFU48611.1};
RN [1] {ECO:0000313|EMBL:AFU48611.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TP-7 {ECO:0000313|EMBL:AFU48611.1};
RX PubMed=23001647; DOI=10.1128/AEM.02114-12;
RA Lee S.J., Lee S.J., Lee Y.J., Kim S.B., Kim S.K., Lee D.W.;
RT "Homologous Alkalophilic and Acidophilic L-Arabinose Isomerases Reveal
RT Region-Specific Contributions to the pH Dependence of Activity and
RT Stability.";
RL Appl. Environ. Microbiol. 78:8813-8816(2012).
RN [2] {ECO:0007829|PDB:7CHL}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 1-131 AND 379-382.
RA Cao T.P., Dhanasingh I., Sung J.Y., Shin S.M., Lee D.W., Lee S.H.;
RT "Crystal structure of hybrid Arabinose isomerase AI-10.";
RL Submitted (JUL-2020) to the PDB data bank.
RN [3] {ECO:0007829|PDB:7CX7}
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 31-31; 132-283 AND 342-342.
RA Hoang N.K.Q., Dhanasingh I., Cao T.P., Sung J.Y., Shin S.M., Lee D.W.,
RA Lee S.H.;
RT "Crystal structure of Arabinose isomerase from hyper thermophilic bacterium
RT Thermotoga maritima (TMAI) wt.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [4] {ECO:0007829|PDB:7CXO}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-131 AND 379-382.
RA Hoang N.K.Q., Dhanasingh I., Cao T.P., Sung J.Y., Shin S.M., Lee D.W.,
RA Lee S.H.;
RT "Crystal structure of Arabinose isomerase from hyper thermophilic hybrid
RT AI10.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [5] {ECO:0007829|PDB:7CYY}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 31-31; 132-283 AND 342-342.
RA Hoang N.K.Q., Dhanasingh I., Cao T.P., Sung J.Y., Shin S.M., Lee D.W.,
RA Lee S.H.;
RT "Crystal structure of Arabinose isomerase from hyper thermophilic hybrid
RT AI8 with Adonitol.";
RL Submitted (SEP-2020) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00519};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00519};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00519}.
CC -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC {ECO:0000256|HAMAP-Rule:MF_00519}.
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DR EMBL; JQ945232; AFU48611.1; -; Genomic_DNA.
DR PDB; 7CHL; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-131, A/B/C/D/E/F/G/H/I/J/K/L=379-382.
DR PDB; 7CX7; X-ray; 2.49 A; A/B/C/D/E/F=132-283, A/B/C/D/E/F=342-342.
DR PDB; 7CXO; X-ray; 3.20 A; A/B/C/D/E/F=1-131.
DR PDB; 7CYY; X-ray; 2.60 A; A/B/C/D/E/F=31-31, A/B/C/D/E/F=132-283, A/B/C/D/E/F=342-342.
DR AlphaFoldDB; K0IGW6; -.
DR SMR; K0IGW6; -.
DR UniPathway; UPA00145; UER00565.
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 CDD; cd03557; L-arabinose_isomerase; 1.
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; L-ARABINOSE ISOMERASE; 1.
DR PANTHER; PTHR38464:SF1; L-ARABINOSE ISOMERASE; 1.
DR Pfam; PF11762; Arabinose_Iso_C; 1.
DR Pfam; PF02610; Arabinose_Isome; 1.
DR PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR SUPFAM; SSF50443; FucI/AraA C-terminal domain-like; 1.
DR SUPFAM; SSF53743; FucI/AraA N-terminal and middle domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7CHL, ECO:0007829|PDB:7CX7};
KW Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935, ECO:0000256|HAMAP-
KW Rule:MF_00519};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00519};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00519};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00519};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00519}.
FT DOMAIN 359..472
FT /note="L-arabinose isomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11762"
FT BINDING 305
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 330
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 446
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
SQ SEQUENCE 494 AA; 54944 MW; C4D4A5BC41EB5698 CRC64;
MKMPAYEFWF VVGSQHLYGD EALAQVEAHA REMVPALQAA VGNAHVLRWK GVLKDADEIR
RLCLEASADD VCAGVIAWMH TFSPAKMWIR GLLALRKPLL HLHTQFNRDI PWDTIDMDFM
NLNQSAHGDR EFGFMVTRLG MPRKVIVGHW QDAEVARRVR GWAMTAVAAA VSRGLKVARF
GDNMRQVAVT EGDKVEAEAR FGWSVNGYGV GDLAERVRAV SEAEIDRLID EYQSLYEFAP
GCEKGGPLHD GVREQARIEL GLRSFLEEGG FEAFTTTFED LHGLRQLPGL AVQRLMADGY
GFGGEGDWKT AVFVRVLKVL AEGEGTSFME DYTYHFEPGN EMVLGAHMLE VCPTIAATRP
RVEVHPLSIG GKEDPARLVF DGAGGPAVQA TIVDLGHRFR MVVNKVEAIQ PDRPMPKLPV
ARVLWKPLPS LASAAESWIL AGGAHHTVFS YRVTVEELQD LADMMGMECV VIDEHSTPRR
IANELRWNEA VYGR
//
