ID   ARAA_MYCSM              Reviewed;         501 AA.
AC   Q9RHG2;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 73.
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};
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SMDU;
RA   Soda A., Takata G., Izumori K.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
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; AB036736; BAA89428.1; -; Genomic_DNA.
DR   EMBL; AB038527; BAA92526.1; -; Genomic_DNA.
DR   RefSeq; WP_011727846.1; NZ_UGQO01000001.1.
DR   AlphaFoldDB; Q9RHG2; -.
DR   SMR; Q9RHG2; -.
DR   GeneID; 66733163; -.
DR   OMA; HMLEICP; -.
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   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.
FT   CHAIN           1..501
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_0000198390"
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         449
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ   SEQUENCE   501 AA;  54955 MW;  FD2CFFE85A2ED960 CRC64;
     MAEHFTDEEI WFVTGSQSLY GQEILDQVAE QSRALAERLD ASADLPVAVR WKPVVTTSEA
     ILDVLRDASS SPQCVGVITW MHTFSPAKMW IRGLSALQKP MLHLHTQFGV EIPWDTIDMD
     FMNLNQAAHG DREFGYIQTR LSVPRTTVAG HVGDPRTTAR IGSWMRAALG AAELRSLRIA
     RFGDNMRDVA VTEGDKVEAE SHFGVSVNTY SVNDLAKAVY DVSDPEIDKL VQEYEDTYAV
     AEELRRGGER HASLREGARI ELGLRHFLAD GFGAFTTNFE DLGDLRQLPG LAVQRLMADG
     FGFGAEGDWK TSAMVRTVKT MGVGLPGGTS FMEDYTYDLT PGSERILGAH MLEVCPSIAG
     QTPSLEVHPL GIGNREDPVR LRFTAAPGSG VVLGICDMGS RFRLVANHVT VVEPSAPLPN
     LPVACAVWEP EPSWSTSTEA WLMAGGPHHT VLTTAVSPTT LDDFATITGT ELLQIDQHTT
     PREFQREMRW NAVYHHIAAG L