ID   ARAA2_CLOAB             Reviewed;         488 AA.
AC   Q97JE0;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=L-arabinose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00519};
DE            EC=5.3.1.4 {ECO:0000255|HAMAP-Rule:MF_00519};
GN   Name=araA2 {ECO:0000255|HAMAP-Rule:MF_00519}; OrderedLocusNames=CA_C1346;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79314.1; -; Genomic_DNA.
DR   PIR; G97065; G97065.
DR   RefSeq; NP_347974.1; NC_003030.1.
DR   RefSeq; WP_010964655.1; NC_003030.1.
DR   AlphaFoldDB; Q97JE0; -.
DR   SMR; Q97JE0; -.
DR   STRING; 272562.CA_C1346; -.
DR   DNASU; 1117529; -.
DR   EnsemblBacteria; AAK79314; AAK79314; CA_C1346.
DR   GeneID; 44997851; -.
DR   KEGG; cac:CA_C1346; -.
DR   PATRIC; fig|272562.8.peg.1551; -.
DR   eggNOG; COG2160; Bacteria.
DR   HOGENOM; CLU_045663_0_0_9; -.
DR   OMA; REYAFIN; -.
DR   OrthoDB; 507566at2; -.
DR   BRENDA; 5.3.1.4; 1452.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000000814; 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..488
FT                   /note="L-arabinose isomerase 2"
FT                   /id="PRO_0000198384"
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   488 AA;  55487 MW;  2453F45FE4849FF3 CRC64;
     MLENKKMEFW FVVGSQHLYG EEALKEVRKN SETIVDELNK SANLPYKIIF KDLATSADKI
     KEIMKEVNYR DEVAGVITWM HTFSPAKMWI AGTKILQKPL LHFATQYNEN IPWKTIDMDY
     MNLHQSAHGD REYGFINARL KKHNKVVVGY WKDKEVQKQV SDWMKVAAGY IASESIKVAR
     FGDNMRNVAV TEGDKVEAQI QFGWTVDYFG IGDLVAEMDK VSQDEINKTY EEFKDLYILD
     PGENDPAFYE KQVKEQIKIE IGLRRFLEKG NYNAFTTNFE DLYGMKQLPG LAVQRLNAEG
     YGFAGEGDWK TAALDRLLKV MTNNTATGFM EDYTYELSRG NEKALGAHML EVDPTFASDK
     PKVIVKPLGI GDKEDPARLI FNGSTGKGVA VSMLDLGTHY RLIINGLTAV KPDEDMPNLP
     VAKMVWKPEP NFIEGVKSWI YAGGGHHTVV SLELTVEQVY DWSRMVGLEA VIIDKDTKLR
     DIIEKTTK