ID   ARALA_AZOBR             Reviewed;         300 AA.
AC   Q1JUP5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=L-arabinolactonase;
DE            EC=3.1.1.15;
GN   Name=araB;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, AND PATHWAY.
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=16950779; DOI=10.1074/jbc.m606727200;
RA   Watanabe S., Shimada N., Tajima K., Kodaki T., Makino K.;
RT   "Identification and characterization of L-arabonate dehydratase, L-2-keto-
RT   3-deoxyarabonate dehydratase and L-arabinolactonase involved in an
RT   alternative pathway of L-arabinose metabolism: novel evolutionary insight
RT   into sugar metabolism.";
RL   J. Biol. Chem. 281:33521-33536(2006).
RN   [2]
RP   PATHWAY.
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=6798025; DOI=10.1128/jb.149.1.364-367.1982;
RA   Novick N.J., Tyler M.E.;
RT   "L-arabinose metabolism in Azospirillum brasiliense.";
RL   J. Bacteriol. 149:364-367(1982).
CC   -!- FUNCTION: Catalyzes the cleavage of L-arabino-gamma-lactone to L-
CC       arabonate. Is involved in a degradation pathway of L-arabinose that
CC       allows A.brasilense to grow on L-arabinose as a sole carbon source. Can
CC       also use D-galactono-1,4-lactone as substrate in vitro; however, the
CC       enzyme is probably not involved in the metabolism of D-galactose in
CC       vivo. {ECO:0000269|PubMed:16950779}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arabinono-1,4-lactone = H(+) + L-arabinonate;
CC         Xref=Rhea:RHEA:16217, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16501, ChEBI:CHEBI:17100; EC=3.1.1.15;
CC         Evidence={ECO:0000269|PubMed:16950779};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
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DR   EMBL; AB241136; BAE94275.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1JUP5; -.
DR   SMR; Q1JUP5; -.
DR   GO; GO:0050021; F:L-arabinonolactonase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019570; P:L-arabinose catabolic process to 2-oxoglutarate; IDA:UniProtKB.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR013658; SGL.
DR   InterPro; IPR005511; SMP-30.
DR   Pfam; PF08450; SGL; 1.
DR   PRINTS; PR01790; SMP30FAMILY.
PE   1: Evidence at protein level;
KW   Arabinose catabolism; Carbohydrate metabolism; Hydrolase; Metal-binding.
FT   CHAIN           1..300
FT                   /note="L-arabinolactonase"
FT                   /id="PRO_0000418505"
FT   BINDING         22
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  32300 MW;  EDCD1C00BBACAAEC CRC64;
     MQQIHPAGQA TLLADTRNTL GEGATWCDRT RALYWVDIEG AQLWRCRADG SDLTPWPMPE
     RLACFALTDD PDVLLVGLAT HLAFFDLRSG AFTRIVEVEP ELPTRLNDGR CDGSGAFVFG
     MKDEGAEPPR AVGGFYRLNA DLTLERLALP PAAIANSIGF SPDGSKMYFC DSLVREIFVC
     DYRPGGEVAN VRPFARLTDP DGDPDGSIVD RDGGLWNAQW GGRRVVRYGP DGVETDRVAV
     PTAQPSCTAL DGEGRLYVTS ARVGLSDDAL ADDPHAGGVF VAQTRHAGMA TARFAGTPRG